5mc4 - Revision history

OCA at 18:38, 1 November 2023

OCA — Wed, 01 Nov 2023 18:38:01 GMT

←Older revision		Revision as of 18:38, 1 November 2023
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	<StructureSection load='5mc4' size='340' side='right'caption='[[5mc4]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='5mc4' size='340' side='right'caption='[[5mc4]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5mc4]] is a 2 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=5MC4 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5MC4 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5mc4]] is a 2 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=5MC4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MC4 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</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">[[5m4j\|5m4j]], [[5mby\|5mby]], [[5mbz\|5mbz]], [[5mc0\|5mc0]], [[5mc1\|5mc1]], [[5mc2\|5mc2]], [[5mc3\|5mc3]], [[5mc5\|5mc5]]</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PEPD, PRD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5mc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mc4 OCA], [https://pdbe.org/5mc4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mc4 RCSB], [https://www.ebi.ac.uk/pdbsum/5mc4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mc4 ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xaa-Pro_dipeptidase Xaa-Pro dipeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.13.9 3.4.13.9] </span></td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5mc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mc4 OCA], [~~http~~://pdbe.org/5mc4 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5mc4 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5mc4 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5mc4 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/PEPD_HUMAN PEPD_HUMAN]] Defects in PEPD are a cause of prolidase deficiency (PD) [MIM:[~~http~~://omim.org/entry/170100 170100]]. Prolidase deficiency is an autosomal recessive disorder associated with iminodipeptiduria. The clinical phenotype includes skin ulcers, mental retardation, recurrent infections, and a characteristic facies. These features, however are incompletely penetrant and highly variable in both age of onset and severity. There is a tight linkage between the polymorphisms of prolidase and the myotonic dystrophy trait.<ref>PMID:2365824</ref> <ref>PMID:8198124</ref> <ref>PMID:8900231</ref> <ref>PMID:12384772</ref>	+	[https://www.uniprot.org/uniprot/PEPD_HUMAN PEPD_HUMAN] Defects in PEPD are a cause of prolidase deficiency (PD) [MIM:[https://omim.org/entry/170100 170100]. Prolidase deficiency is an autosomal recessive disorder associated with iminodipeptiduria. The clinical phenotype includes skin ulcers, mental retardation, recurrent infections, and a characteristic facies. These features, however are incompletely penetrant and highly variable in both age of onset and severity. There is a tight linkage between the polymorphisms of prolidase and the myotonic dystrophy trait.<ref>PMID:2365824</ref> <ref>PMID:8198124</ref> <ref>PMID:8900231</ref> <ref>PMID:12384772</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PEPD_HUMAN PEPD_HUMAN]] Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because the high level of iminoacids in collagen.	+	[https://www.uniprot.org/uniprot/PEPD_HUMAN PEPD_HUMAN] Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because the high level of iminoacids in collagen.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 27:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Xaa-Pro dipeptidase]]~~	+	[[Category: Dobbek H]]
-	[[Category: Dobbek, H]]	+	[[Category: Mueller U]]
-	[[Category: Mueller, U]]	+	[[Category: Weiss MS]]
-	[[Category: Weiss~~, M S~~]]	+	[[Category: Wilk P]]
-	[[Category: Wilk, P]]	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Hydrolysis]]~~	+
-	~~[[Category: Metalloenzyme]]~~	+
-	~~[[Category: Mutation]]~~	+
-	~~[[Category: Peptidase]]~~	+
-	~~[[Category: Pita-bread]]~~	+
-	~~[[Category: Prolidase~~]]	+

OCA at 05:55, 22 April 2020

OCA — Wed, 22 Apr 2020 05:55:25 GMT

←Older revision		Revision as of 05:55, 22 April 2020
Line 1:		Line 1:

	==Crystal Structure of Gly448Arg mutant of Human Prolidase with Mn ions and GlyPro ligand==		==Crystal Structure of Gly448Arg mutant of Human Prolidase with Mn ions and GlyPro ligand==
-	<StructureSection load='5mc4' size='340' side='right' caption='[[5mc4]], [[Resolution\|resolution]] 1.80Å' scene=''>	+	<StructureSection load='5mc4' size='340' side='right'caption='[[5mc4]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5mc4]] is a 2 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=5MC4 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5MC4 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5mc4]] is a 2 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=5MC4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5MC4 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5m4j\|5m4j]], [[5mby\|5mby]], [[5mbz\|5mbz]], [[5mc0\|5mc0]], [[5mc1\|5mc1]], [[5mc2\|5mc2]], [[5mc3\|5mc3]], [[5mc5\|5mc5]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5m4j\|5m4j]], [[5mby\|5mby]], [[5mbz\|5mbz]], [[5mc0\|5mc0]], [[5mc1\|5mc1]], [[5mc2\|5mc2]], [[5mc3\|5mc3]], [[5mc5\|5mc5]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PEPD, PRD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PEPD, PRD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xaa-Pro_dipeptidase Xaa-Pro dipeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.13.9 3.4.13.9] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xaa-Pro_dipeptidase Xaa-Pro dipeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.13.9 3.4.13.9] </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=5mc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mc4 OCA], [http://pdbe.org/5mc4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mc4 RCSB], [http://www.ebi.ac.uk/pdbsum/5mc4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mc4 ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5mc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mc4 OCA], [http://pdbe.org/5mc4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mc4 RCSB], [http://www.ebi.ac.uk/pdbsum/5mc4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mc4 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 28:		Line 28:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Xaa-Pro dipeptidase]]		[[Category: Xaa-Pro dipeptidase]]
	[[Category: Dobbek, H]]		[[Category: Dobbek, H]]

OCA at 16:30, 15 August 2018

OCA — Wed, 15 Aug 2018 16:30:34 GMT

←Older revision		Revision as of 16:30, 15 August 2018
Line 3:		Line 3:
	<StructureSection load='5mc4' size='340' side='right' caption='[[5mc4]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='5mc4' size='340' side='right' caption='[[5mc4]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5mc4]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MC4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MC4 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5mc4]] is a 2 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=5MC4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MC4 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5m4j\|5m4j]], [[5mby\|5mby]], [[5mbz\|5mbz]], [[5mc0\|5mc0]], [[5mc1\|5mc1]], [[5mc2\|5mc2]], [[5mc3\|5mc3]], [[5mc5\|5mc5]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5m4j\|5m4j]], [[5mby\|5mby]], [[5mbz\|5mbz]], [[5mc0\|5mc0]], [[5mc1\|5mc1]], [[5mc2\|5mc2]], [[5mc3\|5mc3]], [[5mc5\|5mc5]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PEPD, PRD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xaa-Pro_dipeptidase Xaa-Pro dipeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.13.9 3.4.13.9] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xaa-Pro_dipeptidase Xaa-Pro dipeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.13.9 3.4.13.9] </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=5mc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mc4 OCA], [http://pdbe.org/5mc4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mc4 RCSB], [http://www.ebi.ac.uk/pdbsum/5mc4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mc4 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=5mc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mc4 OCA], [http://pdbe.org/5mc4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mc4 RCSB], [http://www.ebi.ac.uk/pdbsum/5mc4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mc4 ProSAT]</span></td></tr>
Line 13:		Line 14:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/PEPD_HUMAN PEPD_HUMAN]] Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because the high level of iminoacids in collagen.		[[http://www.uniprot.org/uniprot/PEPD_HUMAN PEPD_HUMAN]] Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because the high level of iminoacids in collagen.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Prolidase is a metallopeptidase that cleaves iminodipeptides containing a proline (Pro) or hydroxyproline (Hyp) residue at their C-terminal end. The disease prolidase deficiency (PD) is a rare recessive human disorder characterized by reduced prolidase activity. PD manifests itself by a wide range of severe clinical symptoms, most commonly as skin ulceration, recurrent infections of the respiratory tract, and mental retardation. Several mutations in the PEPD gene have been identified that are responsible for the loss or the reduction of prolidase activity. In contrast, the structural basis of enzyme inactivation has so far remained elusive. In this study, we present high resolution crystal structures of a number of human prolidase (HsProl) variants, in which single amino acids are either substituted by others or deleted. The observed implications of the mutations on the three-dimensional structure of HsProl are reported and discussed and related to their enzymatic activity. The resulting structures may be divided into four groups depending on the presumed effect of the corresponding mutations on the reaction mechanism. The four possible inactivation mechanisms, which could be elucidated, are disruption of the catalytic Mn2 (OH(-) )-center, introduction of chain disorder along with the displacement of important active site residues, rigidification of the active site, and flexibilization of the active site. DATABASE: All refined structure coordinates as well as the corresponding structure factor amplitudes have been deposited in the PDB under the accession numbers 5MBY, 5MBZ, 5MC0, 5MC1, 5MC2, 5MC3, 5MC4, 5MC5, 6H2P, 6H2Q.
		+
		+	Structural basis for prolidase deficiency disease mechanisms.,Wilk P, Uehlein M, Piwowarczyk R, Dobbek H, Mueller U, Weiss MS FEBS J. 2018 Aug 1. doi: 10.1111/febs.14620. PMID:30066404<ref>PMID:30066404</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5mc4" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Xaa-Pro dipeptidase]]		[[Category: Xaa-Pro dipeptidase]]
	[[Category: Dobbek, H]]		[[Category: Dobbek, H]]

OCA at 06:07, 20 December 2017

OCA — Wed, 20 Dec 2017 06:07:06 GMT

←Older revision		Revision as of 06:07, 20 December 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5mc4 is ~~ON HOLD~~	+	==Crystal Structure of Gly448Arg mutant of Human Prolidase with Mn ions and GlyPro ligand==
-		+	<StructureSection load='5mc4' size='340' side='right' caption='[[5mc4]], [[Resolution\|resolution]] 1.80Å' scene=''>
-	~~Authors~~: ~~Wilk~~, P., ~~Mueller~~, U., ~~Dobbek~~, H., ~~Weiss~~, M.S.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5mc4]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MC4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MC4 FirstGlance]. <br>
-	~~Description~~: ~~Crystal Structure~~ of ~~Gly448Arg mutant of Human~~ Prolidase with ~~Mn ions~~ and ~~GlyPro ligand~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5m4j\|5m4j]], [[5mby\|5mby]], [[5mbz\|5mbz]], [[5mc0\|5mc0]], [[5mc1\|5mc1]], [[5mc2\|5mc2]], [[5mc3\|5mc3]], [[5mc5\|5mc5]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xaa-Pro_dipeptidase Xaa-Pro dipeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.13.9 3.4.13.9] </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=5mc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mc4 OCA], [http://pdbe.org/5mc4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mc4 RCSB], [http://www.ebi.ac.uk/pdbsum/5mc4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mc4 ProSAT]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/PEPD_HUMAN PEPD_HUMAN]] Defects in PEPD are a cause of prolidase deficiency (PD) [MIM:[http://omim.org/entry/170100 170100]]. Prolidase deficiency is an autosomal recessive disorder associated with iminodipeptiduria. The clinical phenotype includes skin ulcers, mental retardation, recurrent infections, and a characteristic facies. These features, however are incompletely penetrant and highly variable in both age of onset and severity. There is a tight linkage between the polymorphisms of prolidase and the myotonic dystrophy trait.<ref>PMID:2365824</ref> <ref>PMID:8198124</ref> <ref>PMID:8900231</ref> <ref>PMID:12384772</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PEPD_HUMAN PEPD_HUMAN]] Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because the high level of iminoacids in collagen.
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Xaa-Pro dipeptidase]]
	[[Category: Dobbek, H]]		[[Category: Dobbek, H]]
		+	[[Category: Mueller, U]]
		+	[[Category: Weiss, M S]]
	[[Category: Wilk, P]]		[[Category: Wilk, P]]
-	[[Category: ~~Mueller, U~~]]	+	[[Category: Hydrolase]]
-	[[Category: ~~Weiss, M.S~~]]	+	[[Category: Hydrolysis]]
		+	[[Category: Metalloenzyme]]
		+	[[Category: Mutation]]
		+	[[Category: Peptidase]]
		+	[[Category: Pita-bread]]
		+	[[Category: Prolidase]]

OCA: Protected "5mc4" [edit=sysop:move=sysop]

OCA — Fri, 09 Dec 2016 16:37:34 GMT

Protected "5mc4" [edit=sysop:move=sysop]

←Older revision

Revision as of 16:37, 9 December 2016

OCA: New page: '''Unreleased structure''' The entry 5mc4 is ON HOLD Authors: Wilk, P., Mueller, U., Dobbek, H., Weiss, M.S. Description: Crystal Structure of Gly448Arg mutant of Human Prolidase with ...

OCA — Fri, 09 Dec 2016 16:37:33 GMT

New page: '''Unreleased structure''' The entry 5mc4 is ON HOLD Authors: Wilk, P., Mueller, U., Dobbek, H., Weiss, M.S. Description: Crystal Structure of Gly448Arg mutant of Human Prolidase with ...

New page

'''Unreleased structure'''

The entry 5mc4 is ON HOLD

Authors: Wilk, P., Mueller, U., Dobbek, H., Weiss, M.S.

Description: Crystal Structure of Gly448Arg mutant of Human Prolidase with Mn ions and GlyPro ligand
[[Category: Unreleased Structures]]
[[Category: Dobbek, H]]
[[Category: Wilk, P]]
[[Category: Mueller, U]]
[[Category: Weiss, M.S]]