1c22 - Revision history

OCA at 06:40, 7 February 2024

OCA — Wed, 07 Feb 2024 06:40:30 GMT

←Older revision		Revision as of 06:40, 7 February 2024
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	<StructureSection load='1c22' size='340' side='right'caption='[[1c22]], [[Resolution\|resolution]] 1.75Å' scene=''>		<StructureSection load='1c22' size='340' side='right'caption='[[1c22]], [[Resolution\|resolution]] 1.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1c22]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"bacillus_coli"_migula_1895 "bacillus~~ coli~~" migula 1895~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C22 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C22 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1c22]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C22 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C22 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=MF3:2~~-~~AMINO-4-TRIFLUOROMETHYLSULFANYL-BUTYRIC+ACID'>MF3</scene>~~, ~~<scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.75Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[1mat\|1mat]], [[2mat\|2mat]], [[3mat\|3mat]], [[4mat\|4mat]], [[1c21\|1c21]], [[1c23\|1c23]], [[1c24\|1c24]], [[1c27\|1c27]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=MF3:2-AMINO-4-TRIFLUOROMETHYLSULFANYL-BUTYRIC+ACID'>MF3</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[https://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18]~~ </~~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=1c22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c22 OCA], [https://pdbe.org/1c22 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c22 RCSB], [https://www.ebi.ac.uk/pdbsum/1c22 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c22 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=1c22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c22 OCA], [https://pdbe.org/1c22 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c22 RCSB], [https://www.ebi.ac.uk/pdbsum/1c22 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c22 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/~~AMPM_ECOLI AMPM_ECOLI]~~] Removes the N-terminal methionine from nascent proteins.	+	[https://www.uniprot.org/uniprot/MAP1_ECOLI MAP1_ECOLI] Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.[HAMAP-Rule:MF_01974]<ref>PMID:20521764</ref> <ref>PMID:3027045</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=1c22 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=1c22 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	In an effort to differentiate between alternative mechanistic schemes that have been postulated for Escherichia coli methionine aminopeptidase (eMetAP), the modes of binding of a series of products and phosphorus-based transition-state analogues were determined by X-ray crystallography. Methionine phosphonate, norleucine phosphonate, and methionine phosphinate bind with the N-terminal group interacting with Co2 and with the respective phosphorus oxygens binding between the metals, interacting in a bifurcated manner with Co1 and His178 and hydrogen bonded to His79. In contrast, the reaction product methionine and its analogue trifluoromethionine lose interactions with Co1 and His79. The interactions with the transition-state analogues are, in general, very similar to those seen previously for the complex of the enzyme with a bestatin-based inhibitor. The mode of interaction of His79 is, however, different. In the case of the bestatin-based inhibitor, His79 interacts with atoms in the peptide bond between the P(1)' and P(2)' residues. In the present transition-state analogues, however, the histidine moves 1.2 A toward the metal center and hydrogen bonds with the atom that corresponds to the nitrogen of the scissile peptide bond (i.e., between the P(1) and P(1)' residues). These observations tend to support one of the mechanistic schemes for eMetAP considered before, although with a revision in the role played by His79. The results also suggest parallels between the mechanism of action of methionine aminopeptidase and other "pita-bread" enzymes including aminopeptidase P and creatinase.
-
-	Insights into the mechanism of Escherichia coli methionine aminopeptidase from the structural analysis of reaction products and phosphorus-based transition-state analogues.,Lowther WT, Zhang Y, Sampson PB, Honek JF, Matthews BW Biochemistry. 1999 Nov 9;38(45):14810-9. PMID:10555963<ref>PMID:10555963</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1c22" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bacillus~~ coli ~~migula 1895~~]]	+	[[Category: Escherichia coli]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Methionyl aminopeptidase]]~~	+	[[Category: Honek JF]]
-	[[Category: Honek~~, J F~~]]	+	[[Category: Lowther WT]]
-	[[Category: Lowther~~, W T~~]]	+	[[Category: Matthews BW]]
-	[[Category: Matthews~~, B W~~]]	+	[[Category: Sampson PB]]
-	[[Category: Sampson~~, P B~~]]	+	[[Category: Zhang Y]]
-	[[Category: Zhang, Y]]	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Product complex~~]]	+

OCA at 14:49, 3 November 2021

OCA — Wed, 03 Nov 2021 14:49:46 GMT

←Older revision		Revision as of 14:49, 3 November 2021
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	<StructureSection load='1c22' size='340' side='right'caption='[[1c22]], [[Resolution\|resolution]] 1.75Å' scene=''>		<StructureSection load='1c22' size='340' side='right'caption='[[1c22]], [[Resolution\|resolution]] 1.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1c22]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C22 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C22 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1c22]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C22 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C22 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=MF3:2-AMINO-4-TRIFLUOROMETHYLSULFANYL-BUTYRIC+ACID'>MF3</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=MF3:2-AMINO-4-TRIFLUOROMETHYLSULFANYL-BUTYRIC+ACID'>MF3</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mat\|1mat]], [[2mat\|2mat]], [[3mat\|3mat]], [[4mat\|4mat]], [[1c21\|1c21]], [[1c23\|1c23]], [[1c24\|1c24]], [[1c27\|1c27]]</div></td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mat\|1mat]], [[2mat\|2mat]], [[3mat\|3mat]], [[4mat\|4mat]], [[1c21\|1c21]], [[1c23\|1c23]], [[1c24\|1c24]], [[1c27\|1c27]]</div></td></tr>
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Bacillus coli migula 1895]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Methionyl aminopeptidase]]		[[Category: Methionyl aminopeptidase]]

OCA at 15:13, 3 March 2021

OCA — Wed, 03 Mar 2021 15:13:23 GMT

←Older revision		Revision as of 15:13, 3 March 2021
Line 3:		Line 3:
	<StructureSection load='1c22' size='340' side='right'caption='[[1c22]], [[Resolution\|resolution]] 1.75Å' scene=''>		<StructureSection load='1c22' size='340' side='right'caption='[[1c22]], [[Resolution\|resolution]] 1.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1c22]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C22 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1C22 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1c22]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C22 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C22 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=MF3:2-AMINO-4-TRIFLUOROMETHYLSULFANYL-BUTYRIC+ACID'>MF3</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=MF3:2-AMINO-4-TRIFLUOROMETHYLSULFANYL-BUTYRIC+ACID'>MF3</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mat\|1mat]], [[2mat\|2mat]], [[3mat\|3mat]], [[4mat\|4mat]], [[1c21\|1c21]], [[1c23\|1c23]], [[1c24\|1c24]], [[1c27\|1c27]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mat\|1mat]], [[2mat\|2mat]], [[3mat\|3mat]], [[4mat\|4mat]], [[1c21\|1c21]], [[1c23\|1c23]], [[1c24\|1c24]], [[1c27\|1c27]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] </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=1c22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c22 OCA], [~~http~~://pdbe.org/1c22 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1c22 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1c22 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1c22 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=1c22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c22 OCA], [https://pdbe.org/1c22 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c22 RCSB], [https://www.ebi.ac.uk/pdbsum/1c22 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c22 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/AMPM_ECOLI AMPM_ECOLI]] Removes the N-terminal methionine from nascent proteins.	+	[[https://www.uniprot.org/uniprot/AMPM_ECOLI AMPM_ECOLI]] Removes the N-terminal methionine from nascent proteins.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 06:56, 29 May 2019

OCA — Wed, 29 May 2019 06:56:12 GMT

←Older revision		Revision as of 06:56, 29 May 2019
Line 1:		Line 1:

	==E. COLI METHIONINE AMINOPEPTIDASE: TRIFLUOROMETHIONINE COMPLEX==		==E. COLI METHIONINE AMINOPEPTIDASE: TRIFLUOROMETHIONINE COMPLEX==
-	<StructureSection load='1c22' size='340' side='right' caption='[[1c22]], [[Resolution\|resolution]] 1.75Å' scene=''>	+	<StructureSection load='1c22' size='340' side='right'caption='[[1c22]], [[Resolution\|resolution]] 1.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1c22]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C22 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1c22]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C22 FirstGlance]. <br>
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c2/1c22_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c2/1c22_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>
Line 32:		Line 32:

	==See Also==		==See Also==
-	*[[Aminopeptidase\|Aminopeptidase]]	+	*[[Aminopeptidase 3D structures\|Aminopeptidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Methionyl aminopeptidase]]		[[Category: Methionyl aminopeptidase]]
	[[Category: Honek, J F]]		[[Category: Honek, J F]]

OCA at 11:09, 24 August 2017

OCA — Thu, 24 Aug 2017 11:09:46 GMT

←Older revision		Revision as of 11:09, 24 August 2017
Line 1:		Line 1:
		+
	==E. COLI METHIONINE AMINOPEPTIDASE: TRIFLUOROMETHIONINE COMPLEX==		==E. COLI METHIONINE AMINOPEPTIDASE: TRIFLUOROMETHIONINE COMPLEX==
	<StructureSection load='1c22' size='340' side='right' caption='[[1c22]], [[Resolution\|resolution]] 1.75Å' scene=''>		<StructureSection load='1c22' size='340' side='right' caption='[[1c22]], [[Resolution\|resolution]] 1.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1c22]] is a 1 chain structure ~~with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C22 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1c22]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C22 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=MF3:2-AMINO-4-TRIFLUOROMETHYLSULFANYL-BUTYRIC+ACID'>MF3</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=MF3:2-AMINO-4-TRIFLUOROMETHYLSULFANYL-BUTYRIC+ACID'>MF3</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mat\|1mat]], [[2mat\|2mat]], [[3mat\|3mat]], [[4mat\|4mat]], [[1c21\|1c21]], [[1c23\|1c23]], [[1c24\|1c24]], [[1c27\|1c27]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mat\|1mat]], [[2mat\|2mat]], [[3mat\|3mat]], [[4mat\|4mat]], [[1c21\|1c21]], [[1c23\|1c23]], [[1c24\|1c24]], [[1c27\|1c27]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] </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=1c22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c22 OCA], [http://pdbe.org/1c22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1c22 RCSB], [http://www.ebi.ac.uk/pdbsum/1c22 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=1c22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c22 OCA], [http://pdbe.org/1c22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1c22 RCSB], [http://www.ebi.ac.uk/pdbsum/1c22 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1c22 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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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=1c22 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 36:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Bacillus coli migula 1895]]
	[[Category: Methionyl aminopeptidase]]		[[Category: Methionyl aminopeptidase]]
	[[Category: Honek, J F]]		[[Category: Honek, J F]]

OCA at 07:29, 11 September 2015

OCA — Fri, 11 Sep 2015 07:29:39 GMT

←Older revision		Revision as of 07:29, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1c22' size='340' side='right' caption='[[1c22]], [[Resolution\|resolution]] 1.75Å' scene=''>		<StructureSection load='1c22' size='340' side='right' caption='[[1c22]], [[Resolution\|resolution]] 1.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1c22]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Escherichia_coli Escherichia~~ coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C22 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1c22]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C22 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=MF3:2-AMINO-4-TRIFLUOROMETHYLSULFANYL-BUTYRIC+ACID'>MF3</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=MF3:2-AMINO-4-TRIFLUOROMETHYLSULFANYL-BUTYRIC+ACID'>MF3</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mat\|1mat]], [[2mat\|2mat]], [[3mat\|3mat]], [[4mat\|4mat]], [[1c21\|1c21]], [[1c23\|1c23]], [[1c24\|1c24]], [[1c27\|1c27]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mat\|1mat]], [[2mat\|2mat]], [[3mat\|3mat]], [[4mat\|4mat]], [[1c21\|1c21]], [[1c23\|1c23]], [[1c24\|1c24]], [[1c27\|1c27]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] </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=1c22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c22 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1c22 RCSB], [http://www.ebi.ac.uk/pdbsum/1c22 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=1c22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c22 OCA], [http://pdbe.org/1c22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1c22 RCSB], [http://www.ebi.ac.uk/pdbsum/1c22 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		Line 28:
	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 1c22" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Escherichia~~ coli]]	+	[[Category: Bacillus coli migula 1895]]
	[[Category: Methionyl aminopeptidase]]		[[Category: Methionyl aminopeptidase]]
	[[Category: Honek, J F]]		[[Category: Honek, J F]]

OCA at 13:14, 25 December 2014

OCA — Thu, 25 Dec 2014 13:14:34 GMT

←Older revision		Revision as of 13:14, 25 December 2014
Line 8:		Line 8:
	<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=1c22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c22 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1c22 RCSB], [http://www.ebi.ac.uk/pdbsum/1c22 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=1c22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c22 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1c22 RCSB], [http://www.ebi.ac.uk/pdbsum/1c22 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/AMPM_ECOLI AMPM_ECOLI]] Removes the N-terminal methionine from nascent proteins.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 08:32, 22 December 2014

OCA — Mon, 22 Dec 2014 08:32:54 GMT

←Older revision		Revision as of 08:32, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1c22]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C22 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1c22]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C22 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=MF3:2-AMINO-4-TRIFLUOROMETHYLSULFANYL-BUTYRIC+ACID'>MF3</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=MF3:2-AMINO-4-TRIFLUOROMETHYLSULFANYL-BUTYRIC+ACID'>MF3</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mat\|1mat]], [[2mat\|2mat]], [[3mat\|3mat]], [[4mat\|4mat]], [[1c21\|1c21]], [[1c23\|1c23]], [[1c24\|1c24]], [[1c27\|1c27]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mat\|1mat]], [[2mat\|2mat]], [[3mat\|3mat]], [[4mat\|4mat]], [[1c21\|1c21]], [[1c23\|1c23]], [[1c24\|1c24]], [[1c27\|1c27]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] </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=1c22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c22 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1c22 RCSB], [http://www.ebi.ac.uk/pdbsum/1c22 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=1c22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c22 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1c22 RCSB], [http://www.ebi.ac.uk/pdbsum/1c22 PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 35:
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Methionyl aminopeptidase]]		[[Category: Methionyl aminopeptidase]]
-	[[Category: Honek, J F.]]	+	[[Category: Honek, J F]]
-	[[Category: Lowther, W T.]]	+	[[Category: Lowther, W T]]
-	[[Category: Matthews, B W.]]	+	[[Category: Matthews, B W]]
-	[[Category: Sampson, P B.]]	+	[[Category: Sampson, P B]]
-	[[Category: Zhang, Y.]]	+	[[Category: Zhang, Y]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Product complex]]		[[Category: Product complex]]

OCA at 16:58, 20 August 2014

OCA — Wed, 20 Aug 2014 16:58:58 GMT

←Older revision		Revision as of 16:58, 20 August 2014
Line 1:		Line 1:
-	[[~~Image:~~1c22.~~png~~\|~~left~~\|200px]]	+	==E. COLI METHIONINE AMINOPEPTIDASE: TRIFLUOROMETHIONINE COMPLEX==
		+	<StructureSection load='1c22' size='340' side='right' caption='[[1c22]], [[Resolution\|resolution]] 1.75Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1c22]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C22 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=MF3:2-AMINO-4-TRIFLUOROMETHYLSULFANYL-BUTYRIC+ACID'>MF3</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mat\|1mat]], [[2mat\|2mat]], [[3mat\|3mat]], [[4mat\|4mat]], [[1c21\|1c21]], [[1c23\|1c23]], [[1c24\|1c24]], [[1c27\|1c27]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] </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=1c22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c22 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1c22 RCSB], [http://www.ebi.ac.uk/pdbsum/1c22 PDBsum]</span></td></tr>
		+	<table>
		+	== 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/c2/1c22_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 ==
		+	In an effort to differentiate between alternative mechanistic schemes that have been postulated for Escherichia coli methionine aminopeptidase (eMetAP), the modes of binding of a series of products and phosphorus-based transition-state analogues were determined by X-ray crystallography. Methionine phosphonate, norleucine phosphonate, and methionine phosphinate bind with the N-terminal group interacting with Co2 and with the respective phosphorus oxygens binding between the metals, interacting in a bifurcated manner with Co1 and His178 and hydrogen bonded to His79. In contrast, the reaction product methionine and its analogue trifluoromethionine lose interactions with Co1 and His79. The interactions with the transition-state analogues are, in general, very similar to those seen previously for the complex of the enzyme with a bestatin-based inhibitor. The mode of interaction of His79 is, however, different. In the case of the bestatin-based inhibitor, His79 interacts with atoms in the peptide bond between the P(1)' and P(2)' residues. In the present transition-state analogues, however, the histidine moves 1.2 A toward the metal center and hydrogen bonds with the atom that corresponds to the nitrogen of the scissile peptide bond (i.e., between the P(1) and P(1)' residues). These observations tend to support one of the mechanistic schemes for eMetAP considered before, although with a revision in the role played by His79. The results also suggest parallels between the mechanism of action of methionine aminopeptidase and other "pita-bread" enzymes including aminopeptidase P and creatinase.

-	~~{{STRUCTURE_1c22\| PDB=1c22 \| SCENE= }}~~	+	Insights into the mechanism of Escherichia coli methionine aminopeptidase from the structural analysis of reaction products and phosphorus-based transition-state analogues.,Lowther WT, Zhang Y, Sampson PB, Honek JF, Matthews BW Biochemistry. 1999 Nov 9;38(45):14810-9. PMID:10555963<ref>PMID:10555963</ref>

-	~~===E. COLI METHIONINE AMINOPEPTIDASE: TRIFLUOROMETHIONINE COMPLEX===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_10555963}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1c22]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Escherichia_coli Escherichia coli]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1C22 OCA].~~	+

	==See Also==		==See Also==
	*[[Aminopeptidase\|Aminopeptidase]]		*[[Aminopeptidase\|Aminopeptidase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:010555963<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Methionyl aminopeptidase]]		[[Category: Methionyl aminopeptidase]]

OCA at 17:06, 20 October 2012

OCA — Sat, 20 Oct 2012 17:06:43 GMT

←Older revision		Revision as of 17:06, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1c22]] is a 1 chain structure ~~of [[Aminopeptidase]]~~ with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C22 OCA].	+	[[1c22]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C22 OCA].

	==See Also==		==See Also==