1ei5 - Revision history

OCA at 07:03, 7 February 2024

OCA — Wed, 07 Feb 2024 07:03:13 GMT

←Older revision		Revision as of 07:03, 7 February 2024
Line 3:		Line 3:
	<StructureSection load='1ei5' size='340' side='right'caption='[[1ei5]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1ei5' size='340' side='right'caption='[[1ei5]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1ei5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Atcc_49188 Atcc 49188~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EI5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EI5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1ei5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brucella_anthropi Brucella anthropi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EI5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EI5 FirstGlance]. <br>
-	</td></tr><tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"~~><span class~~=~~'plainlinks'~~>~~[https://en.wikipedia.org/wiki/D~~-~~stereospecific_aminopeptidase D-stereospecific aminopeptidase]~~, ~~with EC number~~ [~~https://www~~.~~brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.19 3.4.11.19] </span>~~</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]] 1.9Å</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=1ei5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ei5 OCA], [https://pdbe.org/1ei5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ei5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ei5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ei5 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=1ei5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ei5 OCA], [https://pdbe.org/1ei5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ei5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ei5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ei5 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/~~DAP_OCHAN DAP_OCHAN]~~] Hydrolyzes N-terminal residues in D-amino acid-containing peptides.~~[HAMAP-Rule:MF_01960]~~	+	[https://www.uniprot.org/uniprot/DAP_BRUAN DAP_BRUAN] Hydrolyzes N-terminal residues in D-amino acid-containing peptides.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 19:		Line 19:
	</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=1ei5 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=1ei5 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	BACKGROUND: beta-Lactam compounds are the most widely used antibiotics. They inactivate bacterial DD-transpeptidases, also called penicillin-binding proteins (PBPs), involved in cell-wall biosynthesis. The most common bacterial resistance mechanism against beta-lactam compounds is the synthesis of beta-lactamases that hydrolyse beta-lactam rings. These enzymes are believed to have evolved from cell-wall DD-peptidases. Understanding the biochemical and mechanistic features of the beta-lactam targets is crucial because of the increasing number of resistant bacteria. DAP is a D-aminopeptidase produced by Ochrobactrum anthropi. It is inhibited by various beta-lactam compounds and shares approximately 25% sequence identity with the R61 DD-carboxypeptidase and the class C beta-lactamases. RESULTS: The crystal structure of DAP has been determined to 1.9 A resolution using the multiple isomorphous replacement (MIR) method. The enzyme folds into three domains, A, B and C. Domain A, which contains conserved catalytic residues, has the classical fold of serine beta-lactamases, whereas domains B and C are both antiparallel eight-stranded beta barrels. A loop of domain C protrudes into the substrate-binding site of the enzyme. CONCLUSIONS: Comparison of the biochemical properties and the structure of DAP with PBPs and serine beta-lactamases shows that although the catalytic site of the enzyme is very similar to that of beta-lactamases, its substrate and inhibitor specificity rests on residues of domain C. DAP is a new member of the family of penicillin-recognizing proteins (PRPs) and, at the present time, its enzymatic specificity is clearly unique.
-
-	Crystal structure of a D-aminopeptidase from Ochrobactrum anthropi, a new member of the 'penicillin-recognizing enzyme' family.,Bompard-Gilles C, Remaut H, Villeret V, Prange T, Fanuel L, Delmarcelle M, Joris B, Frere J, Van Beeumen J Structure. 2000 Sep 15;8(9):971-80. PMID:10986464<ref>PMID:10986464</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1ei5" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Aminopeptidase 3D structures\|Aminopeptidase 3D structures]]		*[[Aminopeptidase 3D structures\|Aminopeptidase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Atcc 49188]]~~	+	[[Category: Brucella anthropi]]
-	~~[[Category: D-stereospecific aminopeptidase~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Beeumen, J Van]]~~	+	[[Category: Bompard-Gilles C]]
-	[[Category: Bompard-Gilles, C]]	+	[[Category: Fanuel L]]
-	[[Category: Fanuel, L]]	+	[[Category: Frere J-M]]
-	[[Category: Frere, J M]]	+	[[Category: Joris J]]
-	[[Category: Joris, J]]	+	[[Category: Prange T]]
-	[[Category: Prange, T]]	+	[[Category: Remaut H]]
-	[[Category: Remaut, H]]	+	[[Category: Van Beeumen J]]
-	[[Category: ~~Villeret, V~~]]	+	[[Category: Villeret V]]
-	[[Category: ~~Alpha/beta domain]]~~	+
-	~~[[Category: Beta barrel domain]]~~	+
-	~~[[Category: D-aminopeptidase]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Penicillin binding protein~~]]	+

OCA at 09:37, 21 July 2021

OCA — Wed, 21 Jul 2021 09:37:42 GMT

←Older revision		Revision as of 09:37, 21 July 2021
Line 3:		Line 3:
	<StructureSection load='1ei5' size='340' side='right'caption='[[1ei5]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1ei5' size='340' side='right'caption='[[1ei5]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1ei5]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Atcc_49188 Atcc 49188]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EI5 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1EI5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1ei5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_49188 Atcc 49188]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EI5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EI5 FirstGlance]. <br>
-	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/D-stereospecific_aminopeptidase D-stereospecific aminopeptidase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.19 3.4.11.19] </span></td></tr>	+	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/D-stereospecific_aminopeptidase D-stereospecific aminopeptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.19 3.4.11.19] </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=1ei5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ei5 OCA], [~~http~~://pdbe.org/1ei5 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1ei5 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1ei5 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1ei5 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=1ei5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ei5 OCA], [https://pdbe.org/1ei5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ei5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ei5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ei5 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/DAP_OCHAN DAP_OCHAN]] Hydrolyzes N-terminal residues in D-amino acid-containing peptides.[HAMAP-Rule:MF_01960]	+	[[https://www.uniprot.org/uniprot/DAP_OCHAN DAP_OCHAN]] Hydrolyzes N-terminal residues in D-amino acid-containing peptides.[HAMAP-Rule:MF_01960]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 14:35, 16 October 2019

OCA — Wed, 16 Oct 2019 14:35:23 GMT

←Older revision		Revision as of 14:35, 16 October 2019
Line 1:		Line 1:

	==CRYSTAL STRUCTURE OF A D-AMINOPEPTIDASE FROM OCHROBACTRUM ANTHROPI==		==CRYSTAL STRUCTURE OF A D-AMINOPEPTIDASE FROM OCHROBACTRUM ANTHROPI==
-	<StructureSection load='1ei5' size='340' side='right' caption='[[1ei5]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='1ei5' size='340' side='right'caption='[[1ei5]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1ei5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_49188 Atcc 49188]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EI5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EI5 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1ei5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_49188 Atcc 49188]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EI5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EI5 FirstGlance]. <br>
Line 28:		Line 28:
	</div>		</div>
	<div class="pdbe-citations 1ei5" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1ei5" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Aminopeptidase 3D structures\|Aminopeptidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 34:		Line 37:
	[[Category: Atcc 49188]]		[[Category: Atcc 49188]]
	[[Category: D-stereospecific aminopeptidase]]		[[Category: D-stereospecific aminopeptidase]]
		+	[[Category: Large Structures]]
	[[Category: Beeumen, J Van]]		[[Category: Beeumen, J Van]]
	[[Category: Bompard-Gilles, C]]		[[Category: Bompard-Gilles, C]]

OCA at 07:19, 20 December 2017

OCA — Wed, 20 Dec 2017 07:19:42 GMT

←Older revision		Revision as of 07:19, 20 December 2017
Line 1:		Line 1:
		+
	==CRYSTAL STRUCTURE OF A D-AMINOPEPTIDASE FROM OCHROBACTRUM ANTHROPI==		==CRYSTAL STRUCTURE OF A D-AMINOPEPTIDASE FROM OCHROBACTRUM ANTHROPI==
	<StructureSection load='1ei5' size='340' side='right' caption='[[1ei5]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1ei5' size='340' side='right' caption='[[1ei5]], [[Resolution\|resolution]] 1.90Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1ei5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_49188 Atcc 49188]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EI5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EI5 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1ei5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_49188 Atcc 49188]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EI5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EI5 FirstGlance]. <br>
	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-stereospecific_aminopeptidase D-stereospecific aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.19 3.4.11.19] </span></td></tr>		</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-stereospecific_aminopeptidase D-stereospecific aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.19 3.4.11.19] </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=1ei5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ei5 OCA], [http://pdbe.org/1ei5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ei5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ei5 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=1ei5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ei5 OCA], [http://pdbe.org/1ei5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ei5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ei5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ei5 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 12:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ei/1ei5_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ei/1ei5_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 27:		Line 28:
	</div>		</div>
	<div class="pdbe-citations 1ei5" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1ei5" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Aminopeptidase\|Aminopeptidase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 19:32, 9 February 2016

OCA — Tue, 09 Feb 2016 19:32:51 GMT

←Older revision		Revision as of 19:32, 9 February 2016
Line 16:		Line 16:
	<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=1ei5 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 01:23, 11 September 2015

OCA — Fri, 11 Sep 2015 01:23:35 GMT

←Older revision		Revision as of 01:23, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1ei5' size='340' side='right' caption='[[1ei5]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1ei5' size='340' side='right' caption='[[1ei5]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1ei5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Ochrobactrum_anthropi Ochrobactrum anthropi~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EI5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EI5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1ei5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_49188 Atcc 49188]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EI5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EI5 FirstGlance]. <br>
	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-stereospecific_aminopeptidase D-stereospecific aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.19 3.4.11.19] </span></td></tr>		</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-stereospecific_aminopeptidase D-stereospecific aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.19 3.4.11.19] </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=1ei5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ei5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ei5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ei5 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=1ei5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ei5 OCA], [http://pdbe.org/1ei5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ei5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ei5 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 26:		Line 26:
	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 1ei5" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 33:		Line 34:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Atcc 49188]]
	[[Category: D-stereospecific aminopeptidase]]		[[Category: D-stereospecific aminopeptidase]]
-	[[Category: Ochrobactrum anthropi]]
	[[Category: Beeumen, J Van]]		[[Category: Beeumen, J Van]]
	[[Category: Bompard-Gilles, C]]		[[Category: Bompard-Gilles, C]]

OCA at 09:03, 25 December 2014

OCA — Thu, 25 Dec 2014 09:03:34 GMT

←Older revision		Revision as of 09:03, 25 December 2014
Line 6:		Line 6:
	<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=1ei5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ei5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ei5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ei5 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=1ei5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ei5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ei5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ei5 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/DAP_OCHAN DAP_OCHAN]] Hydrolyzes N-terminal residues in D-amino acid-containing peptides.[HAMAP-Rule:MF_01960]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 21:39, 22 December 2014

OCA — Mon, 22 Dec 2014 21:39:34 GMT

←Older revision		Revision as of 21:39, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1ei5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ochrobactrum_anthropi Ochrobactrum anthropi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EI5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EI5 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1ei5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ochrobactrum_anthropi Ochrobactrum anthropi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EI5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EI5 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-stereospecific_aminopeptidase D-stereospecific aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.19 3.4.11.19] </span></td></tr>	+	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-stereospecific_aminopeptidase D-stereospecific aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.19 3.4.11.19] </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=1ei5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ei5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ei5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ei5 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=1ei5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ei5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ei5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ei5 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 33:		Line 33:
	[[Category: D-stereospecific aminopeptidase]]		[[Category: D-stereospecific aminopeptidase]]
	[[Category: Ochrobactrum anthropi]]		[[Category: Ochrobactrum anthropi]]
-	[[Category: Beeumen, J Van.]]	+	[[Category: Beeumen, J Van]]
-	[[Category: Bompard-Gilles, C.]]	+	[[Category: Bompard-Gilles, C]]
-	[[Category: Fanuel, L.]]	+	[[Category: Fanuel, L]]
-	[[Category: Frere, J M.]]	+	[[Category: Frere, J M]]
-	[[Category: Joris, J.]]	+	[[Category: Joris, J]]
-	[[Category: Prange, T.]]	+	[[Category: Prange, T]]
-	[[Category: Remaut, H.]]	+	[[Category: Remaut, H]]
-	[[Category: Villeret, V.]]	+	[[Category: Villeret, V]]
	[[Category: Alpha/beta domain]]		[[Category: Alpha/beta domain]]
	[[Category: Beta barrel domain]]		[[Category: Beta barrel domain]]

OCA at 11:29, 24 September 2014

OCA — Wed, 24 Sep 2014 11:29:30 GMT

←Older revision		Revision as of 11:29, 24 September 2014
Line 1:		Line 1:
-	[[~~Image~~:1ei5.~~png\|left~~\|200px]]	+	==CRYSTAL STRUCTURE OF A D-AMINOPEPTIDASE FROM OCHROBACTRUM ANTHROPI==
		+	<StructureSection load='1ei5' size='340' side='right' caption='[[1ei5]], [[Resolution\|resolution]] 1.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1ei5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ochrobactrum_anthropi Ochrobactrum anthropi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EI5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EI5 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-stereospecific_aminopeptidase D-stereospecific aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.19 3.4.11.19] </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=1ei5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ei5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ei5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ei5 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/ei/1ei5_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 ==
		+	BACKGROUND: beta-Lactam compounds are the most widely used antibiotics. They inactivate bacterial DD-transpeptidases, also called penicillin-binding proteins (PBPs), involved in cell-wall biosynthesis. The most common bacterial resistance mechanism against beta-lactam compounds is the synthesis of beta-lactamases that hydrolyse beta-lactam rings. These enzymes are believed to have evolved from cell-wall DD-peptidases. Understanding the biochemical and mechanistic features of the beta-lactam targets is crucial because of the increasing number of resistant bacteria. DAP is a D-aminopeptidase produced by Ochrobactrum anthropi. It is inhibited by various beta-lactam compounds and shares approximately 25% sequence identity with the R61 DD-carboxypeptidase and the class C beta-lactamases. RESULTS: The crystal structure of DAP has been determined to 1.9 A resolution using the multiple isomorphous replacement (MIR) method. The enzyme folds into three domains, A, B and C. Domain A, which contains conserved catalytic residues, has the classical fold of serine beta-lactamases, whereas domains B and C are both antiparallel eight-stranded beta barrels. A loop of domain C protrudes into the substrate-binding site of the enzyme. CONCLUSIONS: Comparison of the biochemical properties and the structure of DAP with PBPs and serine beta-lactamases shows that although the catalytic site of the enzyme is very similar to that of beta-lactamases, its substrate and inhibitor specificity rests on residues of domain C. DAP is a new member of the family of penicillin-recognizing proteins (PRPs) and, at the present time, its enzymatic specificity is clearly unique.

-	~~{{STRUCTURE_1ei5\| PDB=1ei5 \| SCENE= }}~~	+	Crystal structure of a D-aminopeptidase from Ochrobactrum anthropi, a new member of the 'penicillin-recognizing enzyme' family.,Bompard-Gilles C, Remaut H, Villeret V, Prange T, Fanuel L, Delmarcelle M, Joris B, Frere J, Van Beeumen J Structure. 2000 Sep 15;8(9):971-80. PMID:10986464<ref>PMID:10986464</ref>

-	~~===CRYSTAL STRUCTURE OF A D-AMINOPEPTIDASE FROM OCHROBACTRUM ANTHROPI===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-		+	==See Also==
-	==~~About this Structure~~==	+	*[[Aminopeptidase\|Aminopeptidase]]
-	[[~~1ei5~~]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ochrobactrum_anthropi Ochrobactrum anthropi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EI5 OCA].	+	== References ==
-		+	<references/>
-	==~~Reference~~==	+	__TOC__
-	<~~ref group="xtra">PMID:010986464<~~/~~ref~~><~~references group="xtra"~~/>	+	</StructureSection>
	[[Category: D-stereospecific aminopeptidase]]		[[Category: D-stereospecific aminopeptidase]]
	[[Category: Ochrobactrum anthropi]]		[[Category: Ochrobactrum anthropi]]

OCA: Protected "1ei5" [edit=sysop:move=sysop]

OCA — Thu, 08 Nov 2012 14:41:02 GMT

Protected "1ei5" [edit=sysop:move=sysop]

←Older revision

Revision as of 14:41, 8 November 2012