1kku - Revision history

OCA at 07:25, 14 February 2024

OCA — Wed, 14 Feb 2024 07:25:47 GMT

←Older revision		Revision as of 07:25, 14 February 2024
Line 3:		Line 3:
	<StructureSection load='1kku' size='340' side='right'caption='[[1kku]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='1kku' size='340' side='right'caption='[[1kku]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1kku]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KKU FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1kku]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KKU FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">~~<div style='overflow: auto; max~~-~~height: 3em;'>[[1f9a\|1f9a]]~~, [[~~1ej2~~\|~~1ej2~~]]~~</div></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.5Å</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Nicotinamide-nucleotide_adenylyltransferase Nicotinamide-nucleotide adenylyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.~~7.7.1 2.7.7.1] </span>~~</td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kku OCA], [https://pdbe.org/1kku PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kku RCSB], [https://www.ebi.ac.uk/pdbsum/1kku PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kku ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kku OCA], [https://pdbe.org/1kku PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kku RCSB], [https://www.ebi.ac.uk/pdbsum/1kku PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kku ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/NMNA1_HUMAN NMNA1_HUMAN]] Defects in NMNAT1 are the cause of Leber congenital amaurosis 9 (LCA9) [MIM:[https://omim.org/entry/608553 608553]]. A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus.<ref>PMID:22842230</ref> <ref>PMID:22842231</ref> <ref>PMID:22842229</ref> <ref>PMID:22842227</ref>	+	[https://www.uniprot.org/uniprot/NMNA1_HUMAN NMNA1_HUMAN] Defects in NMNAT1 are the cause of Leber congenital amaurosis 9 (LCA9) [MIM:[https://omim.org/entry/608553 608553]. A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus.<ref>PMID:22842230</ref> <ref>PMID:22842231</ref> <ref>PMID:22842229</ref> <ref>PMID:22842227</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/NMNA1_HUMAN NMNA1_HUMAN]] Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, prefers NAD(+) and NAAD as substrates and degrades NADH, nicotinic acid adenine dinucleotide phosphate (NHD) and nicotinamide guanine dinucleotide (NGD) less effectively. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NAADP(+). Protects against axonal degeneration following mechanical or toxic insults.<ref>PMID:17402747</ref>	+	[https://www.uniprot.org/uniprot/NMNA1_HUMAN NMNA1_HUMAN] Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, prefers NAD(+) and NAAD as substrates and degrades NADH, nicotinic acid adenine dinucleotide phosphate (NHD) and nicotinamide guanine dinucleotide (NGD) less effectively. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NAADP(+). Protects against axonal degeneration following mechanical or toxic insults.<ref>PMID:17402747</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kku ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kku ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Nicotinamide mononucleotide adenylyltransferase (NMNAT), a member of the nucleotidyltransferase alpha/beta-phosphodiesterases superfamily, catalyzes a universal step (NMN + ATP = NAD + PP(i)) in NAD biosynthesis. Localized within the nucleus, the activity of the human enzyme is greatly altered in tumor cells, rendering it a promising target for cancer chemotherapy. By using a combination of single isomorphous replacement and density modification techniques, the human NMNAT structure was solved by x-ray crystallography to a 2.5-A resolution, revealing a hexamer that is composed of alpha/beta-topology subunits. The active site topology of the enzyme, analyzed through homology modeling and structural comparison with other NMNATs, yielded convincing evidence for a substrate-induced conformational change. We also observed remarkable structural conservation in the ATP-recognition motifs GXXXPX(T/H)XXH and SXTXXR, which we take to be the universal signature for NMNATs. Structural comparison of human and prokaryotic NMNATs may also lead to the rational design of highly selective antimicrobial drugs.
-
-	Structure of human NMN adenylyltransferase. A key nuclear enzyme for NAD homeostasis.,Garavaglia S, D'Angelo I, Emanuelli M, Carnevali F, Pierella F, Magni G, Rizzi M J Biol Chem. 2002 Mar 8;277(10):8524-30. Epub 2001 Dec 19. PMID:11751893<ref>PMID:11751893</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1kku" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Nicotinamide-nucleotide adenylyltransferase~~]]	+	[[Category: Carnevali F]]
-	[[Category: Angelo, I ~~D]]~~	+	[[Category: D'Angelo I]]
-	~~[[Category: Carnevali, F~~]]	+	[[Category: Emanuelli M]]
-	[[Category: Emanuelli, M]]	+	[[Category: Garavaglia S]]
-	[[Category: Garavaglia, S]]	+	[[Category: Magni G]]
-	[[Category: Magni, G]]	+	[[Category: Pierella F]]
-	[[Category: Pierella, F]]	+	[[Category: Rizzi M]]
-	[[Category: Rizzi, M]]	+
-	~~[[Category: Alpha/beta structure - rossmann fold]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 06:54, 11 August 2021

OCA — Wed, 11 Aug 2021 06:54:46 GMT

OCA at 09:35, 6 November 2019

OCA — Wed, 06 Nov 2019 09:35:11 GMT

←Older revision		Revision as of 09:35, 6 November 2019
Line 1:		Line 1:

	==Crystal structure of nuclear human nicotinamide mononucleotide adenylyltransferase==		==Crystal structure of nuclear human nicotinamide mononucleotide adenylyltransferase==
-	<StructureSection load='1kku' size='340' side='right' caption='[[1kku]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='1kku' size='340' side='right'caption='[[1kku]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1kku]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KKU FirstGlance]. <br>		<table><tr><td colspan='2'>[[1kku]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KKU FirstGlance]. <br>
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	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Nicotinamide-nucleotide adenylyltransferase]]		[[Category: Nicotinamide-nucleotide adenylyltransferase]]
	[[Category: Angelo, I D]]		[[Category: Angelo, I D]]

OCA at 21:41, 24 January 2018

OCA — Wed, 24 Jan 2018 21:41:30 GMT

←Older revision		Revision as of 21:41, 24 January 2018
Line 1:		Line 1:
		+
	==Crystal structure of nuclear human nicotinamide mononucleotide adenylyltransferase==		==Crystal structure of nuclear human nicotinamide mononucleotide adenylyltransferase==
	<StructureSection load='1kku' size='340' side='right' caption='[[1kku]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='1kku' size='340' side='right' caption='[[1kku]], [[Resolution\|resolution]] 2.50Å' scene=''>
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	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f9a\|1f9a]], [[1ej2\|1ej2]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f9a\|1f9a]], [[1ej2\|1ej2]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nicotinamide-nucleotide_adenylyltransferase Nicotinamide-nucleotide adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.1 2.7.7.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nicotinamide-nucleotide_adenylyltransferase Nicotinamide-nucleotide adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.1 2.7.7.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kku OCA], [http://pdbe.org/1kku PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kku RCSB], [http://www.ebi.ac.uk/pdbsum/1kku PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kku OCA], [http://pdbe.org/1kku PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kku RCSB], [http://www.ebi.ac.uk/pdbsum/1kku PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kku ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 15:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kk/1kku_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kk/1kku_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 03:06, 8 February 2016

OCA — Mon, 08 Feb 2016 03:06:58 GMT

←Older revision		Revision as of 03:06, 8 February 2016
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	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kku ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 07:17, 10 September 2015

OCA — Thu, 10 Sep 2015 07:17:00 GMT

←Older revision		Revision as of 07:17, 10 September 2015
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	<StructureSection load='1kku' size='340' side='right' caption='[[1kku]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='1kku' size='340' side='right' caption='[[1kku]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1kku]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KKU FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1kku]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KKU FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f9a\|1f9a]], [[1ej2\|1ej2]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f9a\|1f9a]], [[1ej2\|1ej2]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nicotinamide-nucleotide_adenylyltransferase Nicotinamide-nucleotide adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.1 2.7.7.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nicotinamide-nucleotide_adenylyltransferase Nicotinamide-nucleotide adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.1 2.7.7.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kku OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kku RCSB], [http://www.ebi.ac.uk/pdbsum/1kku PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kku OCA], [http://pdbe.org/1kku PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kku RCSB], [http://www.ebi.ac.uk/pdbsum/1kku PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1kku" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Nicotinamide-nucleotide adenylyltransferase]]		[[Category: Nicotinamide-nucleotide adenylyltransferase]]
	[[Category: Angelo, I D]]		[[Category: Angelo, I D]]

OCA at 16:02, 5 January 2015

OCA — Mon, 05 Jan 2015 16:02:01 GMT

←Older revision		Revision as of 16:02, 5 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1kku]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KKU FirstGlance]. <br>		<table><tr><td colspan='2'>[[1kku]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KKU FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f9a\|1f9a]], [[1ej2\|1ej2]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f9a\|1f9a]], [[1ej2\|1ej2]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nicotinamide-nucleotide_adenylyltransferase Nicotinamide-nucleotide adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.1 2.7.7.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nicotinamide-nucleotide_adenylyltransferase Nicotinamide-nucleotide adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.1 2.7.7.1] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kku OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kku RCSB], [http://www.ebi.ac.uk/pdbsum/1kku PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kku OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kku RCSB], [http://www.ebi.ac.uk/pdbsum/1kku PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/NMNA1_HUMAN NMNA1_HUMAN]] Defects in NMNAT1 are the cause of Leber congenital amaurosis 9 (LCA9) [MIM:[http://omim.org/entry/608553 608553]]. A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus.<ref>PMID:22842230</ref> <ref>PMID:22842231</ref> <ref>PMID:22842229</ref> <ref>PMID:22842227</ref>		[[http://www.uniprot.org/uniprot/NMNA1_HUMAN NMNA1_HUMAN]] Defects in NMNAT1 are the cause of Leber congenital amaurosis 9 (LCA9) [MIM:[http://omim.org/entry/608553 608553]]. A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus.<ref>PMID:22842230</ref> <ref>PMID:22842231</ref> <ref>PMID:22842229</ref> <ref>PMID:22842227</ref>
Line 35:		Line 35:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Nicotinamide-nucleotide adenylyltransferase]]		[[Category: Nicotinamide-nucleotide adenylyltransferase]]
-	[[Category: Angelo, I D.]]	+	[[Category: Angelo, I D]]
-	[[Category: Carnevali, F.]]	+	[[Category: Carnevali, F]]
-	[[Category: Emanuelli, M.]]	+	[[Category: Emanuelli, M]]
-	[[Category: Garavaglia, S.]]	+	[[Category: Garavaglia, S]]
-	[[Category: Magni, G.]]	+	[[Category: Magni, G]]
-	[[Category: Pierella, F.]]	+	[[Category: Pierella, F]]
-	[[Category: Rizzi, M.]]	+	[[Category: Rizzi, M]]
	[[Category: Alpha/beta structure - rossmann fold]]		[[Category: Alpha/beta structure - rossmann fold]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 16:09, 29 September 2014

OCA — Mon, 29 Sep 2014 16:09:30 GMT

←Older revision		Revision as of 16:09, 29 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1kku~~\| ~~PDB~~=1kku \| ~~SCENE~~= }}	+	==Crystal structure of nuclear human nicotinamide mononucleotide adenylyltransferase==
-	===~~Crystal structure~~ of ~~nuclear human~~ nicotinamide mononucleotide ~~adenylyltransferase~~===	+	<StructureSection load='1kku' size='340' side='right' caption='[[1kku]], [[Resolution\|resolution]] 2.50Å' scene=''>
-	~~{{ABSTRACT_PUBMED_11751893}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1kku]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KKU FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f9a\|1f9a]], [[1ej2\|1ej2]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nicotinamide-nucleotide_adenylyltransferase Nicotinamide-nucleotide adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.1 2.7.7.1] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kku OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kku RCSB], [http://www.ebi.ac.uk/pdbsum/1kku PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/NMNA1_HUMAN NMNA1_HUMAN]] Defects in NMNAT1 are the cause of Leber congenital amaurosis 9 (LCA9) [MIM:[http://omim.org/entry/608553 608553]]. A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus.<ref>PMID:22842230</ref> <ref>PMID:22842231</ref> <ref>PMID:22842229</ref> <ref>PMID:22842227</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/NMNA1_HUMAN NMNA1_HUMAN]] Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, prefers NAD(+) and NAAD as substrates and degrades NADH, nicotinic acid adenine dinucleotide phosphate (NHD) and nicotinamide guanine dinucleotide (NGD) less effectively. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NAADP(+). Protects against axonal degeneration following mechanical or toxic insults.<ref>PMID:17402747</ref>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kk/1kku_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Nicotinamide mononucleotide adenylyltransferase (NMNAT), a member of the nucleotidyltransferase alpha/beta-phosphodiesterases superfamily, catalyzes a universal step (NMN + ATP = NAD + PP(i)) in NAD biosynthesis. Localized within the nucleus, the activity of the human enzyme is greatly altered in tumor cells, rendering it a promising target for cancer chemotherapy. By using a combination of single isomorphous replacement and density modification techniques, the human NMNAT structure was solved by x-ray crystallography to a 2.5-A resolution, revealing a hexamer that is composed of alpha/beta-topology subunits. The active site topology of the enzyme, analyzed through homology modeling and structural comparison with other NMNATs, yielded convincing evidence for a substrate-induced conformational change. We also observed remarkable structural conservation in the ATP-recognition motifs GXXXPX(T/H)XXH and SXTXXR, which we take to be the universal signature for NMNATs. Structural comparison of human and prokaryotic NMNATs may also lead to the rational design of highly selective antimicrobial drugs.

-	~~==Disease==~~	+	Structure of human NMN adenylyltransferase. A key nuclear enzyme for NAD homeostasis.,Garavaglia S, D'Angelo I, Emanuelli M, Carnevali F, Pierella F, Magni G, Rizzi M J Biol Chem. 2002 Mar 8;277(10):8524-30. Epub 2001 Dec 19. PMID:11751893<ref>PMID:11751893</ref>
-	~~[[http://www.uniprot.org/uniprot/NMNA1_HUMAN NMNA1_HUMAN]] Defects in NMNAT1 are the cause~~ of ~~Leber congenital amaurosis 9 (LCA9) [MIM:[http://omim.org/entry/608553 608553]]~~. A ~~severe dystrophy of the retina, typically becoming evident in the first years of life~~. ~~Visual function is usually poor and often accompanied by nystagmus~~, ~~sluggish or near-absent pupillary responses~~, ~~photophobia~~, ~~high hyperopia and keratoconus~~.~~<ref>PMID~~:~~22842230</ref><ref>~~PMID:~~22842231</ref><ref>PMID:22842229</ref>~~<ref>PMID:~~22842227~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www.uniprot.org/uniprot/NMNA1_HUMAN NMNA1_HUMAN]] Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form~~; ~~nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction~~, ~~i.e. the pyrophosphorolytic cleavage~~ of ~~NAD(+). For~~ the ~~pyrophosphorolytic activity, prefers NAD(+) and NAAD as substrates and degrades NADH, nicotinic acid adenine dinucleotide phosphate (NHD) and nicotinamide guanine dinucleotide (NGD) less effectively~~. ~~Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NAADP(+)~~. ~~Protects against axonal degeneration following mechanical or toxic insults~~.<~~ref~~>~~PMID:17402747~~</~~ref~~>	+	</div>
-		+	== References ==
-	==~~About this Structure==~~	+	<references/>
-	[[1kku]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKU OCA].	+	__TOC__
-		+	</StructureSection>
-	~~==Reference~~==	+
-	~~<ref group="xtra">PMID:011751893</ref><ref group="xtra">PMID:011959140</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Nicotinamide-nucleotide adenylyltransferase]]		[[Category: Nicotinamide-nucleotide adenylyltransferase]]

OCA: Protected "1kku" [edit=sysop:move=sysop]

OCA — Mon, 25 Mar 2013 03:54:47 GMT

Protected "1kku" [edit=sysop:move=sysop]

←Older revision

Revision as of 03:54, 25 March 2013

OCA at 03:54, 25 March 2013

OCA — Mon, 25 Mar 2013 03:54:45 GMT

←Older revision		Revision as of 03:54, 25 March 2013
Line 1:		Line 1:
-	{{Seed}}
-	[[Image:1kku.png\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_1kku", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_1kku\| PDB=1kku \| SCENE= }}		{{STRUCTURE_1kku\| PDB=1kku \| SCENE= }}
-
	===Crystal structure of nuclear human nicotinamide mononucleotide adenylyltransferase===		===Crystal structure of nuclear human nicotinamide mononucleotide adenylyltransferase===
		+	{{ABSTRACT_PUBMED_11751893}}

		+	==Disease==
		+	[[http://www.uniprot.org/uniprot/NMNA1_HUMAN NMNA1_HUMAN]] Defects in NMNAT1 are the cause of Leber congenital amaurosis 9 (LCA9) [MIM:[http://omim.org/entry/608553 608553]]. A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus.<ref>PMID:22842230</ref><ref>PMID:22842231</ref><ref>PMID:22842229</ref><ref>PMID:22842227</ref>

-	~~<!--~~	+	==Function==
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_11751893}}, adds the Publication Abstract to the page~~	+	[[http://www.uniprot.org/uniprot/NMNA1_HUMAN NMNA1_HUMAN]] Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, prefers NAD(+) and NAAD as substrates and degrades NADH, nicotinic acid adenine dinucleotide phosphate (NHD) and nicotinamide guanine dinucleotide (NGD) less effectively. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NAADP(+). Protects against axonal degeneration following mechanical or toxic insults.<ref>PMID:17402747</ref>
-	~~(as it appears on PubMed at~~ http://www.~~pubmed~~.~~gov~~), ~~where 11751893 is~~ the ~~PubMed ID number~~.	+
-	-->	+
-	~~{{ABSTRACT_PUBMED_11751893}}~~	+

	==About this Structure==		==About this Structure==
-	~~1KKU~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKU OCA].	+	[[1kku]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKU OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~11751893~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:011751893</ref><ref group="xtra">PMID:011959140</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Nicotinamide-nucleotide adenylyltransferase]]		[[Category: Nicotinamide-nucleotide adenylyltransferase]]
Line 34:		Line 24:
	[[Category: Rizzi, M.]]		[[Category: Rizzi, M.]]
	[[Category: Alpha/beta structure - rossmann fold]]		[[Category: Alpha/beta structure - rossmann fold]]
-		+	[[Category: Transferase]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Mon Feb 16 18:21:29 2009''~~	+

←Older revision		Revision as of 06:54, 11 August 2021
Line 3:		Line 3:
	<StructureSection load='1kku' size='340' side='right'caption='[[1kku]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='1kku' size='340' side='right'caption='[[1kku]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1kku]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKU OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1KKU FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1kku]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KKU FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f9a\|1f9a]], [[1ej2\|1ej2]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1f9a\|1f9a]], [[1ej2\|1ej2]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Nicotinamide-nucleotide_adenylyltransferase Nicotinamide-nucleotide adenylyltransferase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.1 2.7.7.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Nicotinamide-nucleotide_adenylyltransferase Nicotinamide-nucleotide adenylyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.1 2.7.7.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1kku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kku OCA], [~~http~~://pdbe.org/1kku PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1kku RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1kku PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1kku ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kku OCA], [https://pdbe.org/1kku PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kku RCSB], [https://www.ebi.ac.uk/pdbsum/1kku PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kku ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/NMNA1_HUMAN NMNA1_HUMAN]] Defects in NMNAT1 are the cause of Leber congenital amaurosis 9 (LCA9) [MIM:[~~http~~://omim.org/entry/608553 608553]]. A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus.<ref>PMID:22842230</ref> <ref>PMID:22842231</ref> <ref>PMID:22842229</ref> <ref>PMID:22842227</ref>	+	[[https://www.uniprot.org/uniprot/NMNA1_HUMAN NMNA1_HUMAN]] Defects in NMNAT1 are the cause of Leber congenital amaurosis 9 (LCA9) [MIM:[https://omim.org/entry/608553 608553]]. A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus.<ref>PMID:22842230</ref> <ref>PMID:22842231</ref> <ref>PMID:22842229</ref> <ref>PMID:22842227</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/NMNA1_HUMAN NMNA1_HUMAN]] Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, prefers NAD(+) and NAAD as substrates and degrades NADH, nicotinic acid adenine dinucleotide phosphate (NHD) and nicotinamide guanine dinucleotide (NGD) less effectively. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NAADP(+). Protects against axonal degeneration following mechanical or toxic insults.<ref>PMID:17402747</ref>	+	[[https://www.uniprot.org/uniprot/NMNA1_HUMAN NMNA1_HUMAN]] Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, prefers NAD(+) and NAAD as substrates and degrades NADH, nicotinic acid adenine dinucleotide phosphate (NHD) and nicotinamide guanine dinucleotide (NGD) less effectively. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NAADP(+). Protects against axonal degeneration following mechanical or toxic insults.<ref>PMID:17402747</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]