5kgh - Revision history

OCA at 10:00, 27 September 2023

2023-09-27T10:00:31Z

←Older revision		Revision as of 10:00, 27 September 2023
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	<StructureSection load='5kgh' size='340' side='right'caption='[[5kgh]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='5kgh' size='340' side='right'caption='[[5kgh]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5kgh]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Cloab Cloab~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KGH OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5KGH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5kgh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_acetobutylicum_ATCC_824 Clostridium acetobutylicum ATCC 824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KGH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KGH FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene~~>, ~~<scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:~~1~~,2-ETHANEDIOL'>EDO</scene>~~</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]] 1.8Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">~~[[5kf1\|5kf1]], [[5kf2\|5kf2]], [[5kf8\|5kf8]], [[5kf9\|5kf9]], [[5kga\|5kga]], [[5kgj\|5kgj]], [[5kgp\|5kgp]]~~<~~/td~~></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
-	<~~tr id~~='~~gene~~'><~~td class="sblockLbl"~~><~~b>[[Gene\|Gene~~:~~]]</b~~></td>~~<td class="sblockDat">CA_C0184 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272562 CLOAB])~~</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=5kgh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kgh OCA], [https://pdbe.org/5kgh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kgh RCSB], [https://www.ebi.ac.uk/pdbsum/5kgh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kgh ProSAT]</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=5kgh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kgh OCA], [~~http~~://pdbe.org/5kgh PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5kgh RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5kgh PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5kgh ProSAT]</span></td></tr>	+
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/Q97ML2_CLOAB Q97ML2_CLOAB]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Cloab~~]]	+	[[Category: Clostridium acetobutylicum ATCC 824]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Dopkins~~, B J~~]]	+	[[Category: Dopkins BJ]]
-	[[Category: Holden~~, H M~~]]	+	[[Category: Holden HM]]
-	[[Category: Thoden~~, J B~~]]	+	[[Category: Thoden JB]]
-	[[Category: Tipton~~, P A]]~~	+	[[Category: Tipton PA]]
-	~~[[Category: Acyltransferase]]~~	+
-	~~[[Category: Gnat]]~~	+
-	~~[[Category: N-acetyltransferase]]~~	+
-	~~[[Category: Tandem-gnat]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 12:16, 25 December 2019

2019-12-25T12:16:47Z

←Older revision		Revision as of 12:16, 25 December 2019
Line 1:		Line 1:

	==X-ray structure of a glucosamine N-Acetyltransferase from Clostridium acetobutylicum, mutant Y297F==		==X-ray structure of a glucosamine N-Acetyltransferase from Clostridium acetobutylicum, mutant Y297F==
-	<StructureSection load='5kgh' size='340' side='right' caption='[[5kgh]], [[Resolution\|resolution]] 1.80Å' scene=''>	+	<StructureSection load='5kgh' size='340' side='right'caption='[[5kgh]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5kgh]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KGH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KGH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5kgh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cloab Cloab]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KGH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KGH FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5kf1\|5kf1]], [[5kf2\|5kf2]], [[5kf8\|5kf8]], [[5kf9\|5kf9]], [[5kga\|5kga]], [[5kgj\|5kgj]], [[5kgp\|5kgp]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5kf1\|5kf1]], [[5kf2\|5kf2]], [[5kf8\|5kf8]], [[5kf9\|5kf9]], [[5kga\|5kga]], [[5kgj\|5kgj]], [[5kgp\|5kgp]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CA_C0184 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272562 CLOAB])</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=5kgh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kgh OCA], [http://pdbe.org/5kgh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kgh RCSB], [http://www.ebi.ac.uk/pdbsum/5kgh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kgh ProSAT]</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=5kgh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kgh OCA], [http://pdbe.org/5kgh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kgh RCSB], [http://www.ebi.ac.uk/pdbsum/5kgh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kgh ProSAT]</span></td></tr>
	</table>		</table>
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Cloab]]
		+	[[Category: Large Structures]]
	[[Category: Dopkins, B J]]		[[Category: Dopkins, B J]]
	[[Category: Holden, H M]]		[[Category: Holden, H M]]

OCA at 18:04, 13 July 2016

2016-07-13T18:04:32Z

←Older revision		Revision as of 18:04, 13 July 2016
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	<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=5kgh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kgh OCA], [http://pdbe.org/5kgh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kgh RCSB], [http://www.ebi.ac.uk/pdbsum/5kgh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kgh ProSAT]</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=5kgh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kgh OCA], [http://pdbe.org/5kgh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kgh RCSB], [http://www.ebi.ac.uk/pdbsum/5kgh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kgh ProSAT]</span></td></tr>
	</table>		</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Glucosamine/glucosaminide N-acetyltransferase or GlmA catalyzes the transfer of an acetyl group from acetyl CoA to the primary amino group of glucosamine. The enzyme from Clostridium acetobutylicum is thought to be involved in cell wall rescue. In addition to glucosamine, GlmA has been shown to function on di- and trisaccharides of glucosamine as well. Here we present a structural and kinetic analysis of the enzyme. For this investigation, eight structures were determined to resolutions of 2.0 A or better. The overall three-dimensional fold of GlmA places it into the tandem GNAT superfamily. Each subunit of the dimer folds into two distinct domains which exhibit high three-dimensional structural similarity. Whereas both domains bind acetyl CoA, it is the C-terminal domain that is catalytically competent. On the basis of the various structures determined in this investigation, two amino acid residues were targeted for further study: Asp 287 and Tyr 297. Although their positions in the active site suggested that they may play key roles in catalysis by functioning as active site bases and acids, respectively, this was not borne out by characterization of the D287N and Y297F variants. The kinetic properties revealed that both residues were important for substrate binding, but had no critical roles as acid/base catalysts. Kinetic analyses also indicated that GlmA follows an ordered mechanism with acetyl CoA binding first followed by glucosamine. The product, N-acetylglucosamine is then released prior to CoA. The investigation described herein provides significantly new information on enzymes belonging to the tandem GNAT superfamily.
		+
		+	Structural Studies on a Glucosamine/Glucosaminide N-Acetyltransferase.,Dopkins BJ, Tipton PA, Thoden JB, Holden HM Biochemistry. 2016 Jun 27. PMID:27348258<ref>PMID:27348258</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5kgh" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 02:55, 13 July 2016

2016-07-13T02:55:40Z

←Older revision		Revision as of 02:55, 13 July 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5kgh is ~~ON HOLD~~	+	==X-ray structure of a glucosamine N-Acetyltransferase from Clostridium acetobutylicum, mutant Y297F==
-		+	<StructureSection load='5kgh' size='340' side='right' caption='[[5kgh]], [[Resolution\|resolution]] 1.80Å' scene=''>
-	~~Authors~~: ~~Dopkins~~, B.J., ~~Thoden, J~~.B., ~~Tipton~~, P.A., ~~Holden~~, H.M.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5kgh]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KGH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KGH FirstGlance]. <br>
-	~~Description~~: ~~X-ray structure of a glucosamine N-Acetyltransferase from Clostridium acetobutylicum~~, ~~mutant Y297F~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5kf1\|5kf1]], [[5kf2\|5kf2]], [[5kf8\|5kf8]], [[5kf9\|5kf9]], [[5kga\|5kga]], [[5kgj\|5kgj]], [[5kgp\|5kgp]]</td></tr>
-	[[Category: Thoden, J.B]]	+	<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=5kgh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kgh OCA], [http://pdbe.org/5kgh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kgh RCSB], [http://www.ebi.ac.uk/pdbsum/5kgh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kgh ProSAT]</span></td></tr>
-	[[Category: ~~Holden~~, ~~H.M~~]]	+	</table>
-	[[Category: ~~Tipton, P.A~~]]	+	__TOC__
-	[[Category: ~~Dopkins, B.J~~]]	+	</StructureSection>
		+	[[Category: Dopkins, B J]]
		+	[[Category: Holden, H M]]
		+	[[Category: Thoden, J B]]
		+	[[Category: Tipton, P A]]
		+	[[Category: Acyltransferase]]
		+	[[Category: Gnat]]
		+	[[Category: N-acetyltransferase]]
		+	[[Category: Tandem-gnat]]
		+	[[Category: Transferase]]

OCA: Protected "5kgh" [edit=sysop:move=sysop]

2016-06-23T21:34:20Z

Protected "5kgh" [edit=sysop:move=sysop]

←Older revision

Revision as of 21:34, 23 June 2016

OCA: New page: '''Unreleased structure''' The entry 5kgh is ON HOLD Authors: Dopkins, B.J., Thoden, J.B., Tipton, P.A., Holden, H.M. Description: X-ray structure of a glucosamine N-Acetyltransferase ...

2016-06-23T21:34:18Z

New page: '''Unreleased structure''' The entry 5kgh is ON HOLD Authors: Dopkins, B.J., Thoden, J.B., Tipton, P.A., Holden, H.M. Description: X-ray structure of a glucosamine N-Acetyltransferase ...

New page

'''Unreleased structure'''

The entry 5kgh is ON HOLD

Authors: Dopkins, B.J., Thoden, J.B., Tipton, P.A., Holden, H.M.

Description: X-ray structure of a glucosamine N-Acetyltransferase from Clostridium acetobutylicum, mutant Y297F
[[Category: Unreleased Structures]]
[[Category: Thoden, J.B]]
[[Category: Holden, H.M]]
[[Category: Tipton, P.A]]
[[Category: Dopkins, B.J]]