5mc1: Difference between revisions

Revision as of 06:06, 20 December 2017

Crystal Structure of Asp276Asn mutant of Human Prolidase with Mn ions and GlyPro ligand

Structural highlights

5mc1 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	GLY, GOL, MN, NA, PRO
Related:	5m4j, 5mby, 5mbz, 5mc0, 5mc2, 5mc3, 5mc4, 5mc5
Activity:	Xaa-Pro dipeptidase, with EC number 3.4.13.9
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[PEPD_HUMAN] Defects in PEPD are a cause of prolidase deficiency (PD) [MIM: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.^[1] ^[2] ^[3] ^[4]

Function

[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

↑ Tanoue A, Endo F, Kitano A, Matsuda I. A single nucleotide change in the prolidase gene in fibroblasts from two patients with polypeptide positive prolidase deficiency. Expression of the mutant enzyme in NIH 3T3 cells. J Clin Invest. 1990 Jul;86(1):351-5. PMID:2365824 doi:https://dx.doi.org/10.1172/JCI114708
↑ Ledoux P, Scriver C, Hechtman P. Four novel PEPD alleles causing prolidase deficiency. Am J Hum Genet. 1994 Jun;54(6):1014-21. PMID:8198124
↑ Ledoux P, Scriver CR, Hechtman P. Expression and molecular analysis of mutations in prolidase deficiency. Am J Hum Genet. 1996 Nov;59(5):1035-9. PMID:8900231
↑ Forlino A, Lupi A, Vaghi P, Icaro Cornaglia A, Calligaro A, Campari E, Cetta G. Mutation analysis of five new patients affected by prolidase deficiency: the lack of enzyme activity causes necrosis-like cell death in cultured fibroblasts. Hum Genet. 2002 Oct;111(4-5):314-22. Epub 2002 Aug 14. PMID:12384772 doi:10.1007/s00439-002-0792-5

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OCA

[1] Tanoue A, Endo F, Kitano A, Matsuda I. A single nucleotide change in the prolidase gene in fibroblasts from two patients with polypeptide positive prolidase deficiency. Expression of the mutant enzyme in NIH 3T3 cells. J Clin Invest. 1990 Jul;86(1):351-5. PMID:2365824 doi:https://dx.doi.org/10.1172/JCI114708

[2] Ledoux P, Scriver C, Hechtman P. Four novel PEPD alleles causing prolidase deficiency. Am J Hum Genet. 1994 Jun;54(6):1014-21. PMID:8198124

[3] Ledoux P, Scriver CR, Hechtman P. Expression and molecular analysis of mutations in prolidase deficiency. Am J Hum Genet. 1996 Nov;59(5):1035-9. PMID:8900231

[4] Forlino A, Lupi A, Vaghi P, Icaro Cornaglia A, Calligaro A, Campari E, Cetta G. Mutation analysis of five new patients affected by prolidase deficiency: the lack of enzyme activity causes necrosis-like cell death in cultured fibroblasts. Hum Genet. 2002 Oct;111(4-5):314-22. Epub 2002 Aug 14. PMID:12384772 doi:10.1007/s00439-002-0792-5

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[2]

[3]

[4]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5mc1 is ON HOLD
+==Crystal Structure of Asp276Asn mutant of Human Prolidase with Mn ions and GlyPro ligand==
+<StructureSection load='5mc1' size='340' side='right' caption='[[5mc1]], [[Resolution|resolution]] 1.43&Aring;' scene=''>
-Authors: Wilk, P., Mueller, U., Dobbek, H., Weiss, M.S.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5mc1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MC1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MC1 FirstGlance]. <br>
-Description: Crystal Structure of Asp276Asn 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=NA:SODIUM+ION'>NA</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]], [[5mc2|5mc2]], [[5mc3|5mc3]], [[5mc4|5mc4]], [[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=5mc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mc1 OCA], [http://pdbe.org/5mc1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mc1 RCSB], [http://www.ebi.ac.uk/pdbsum/5mc1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mc1 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: Mueller, U]]
+[[Category: Weiss, M S]]
 [[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]]

5mc1: Difference between revisions

Revision as of 06:06, 20 December 2017

Crystal Structure of Asp276Asn mutant of Human Prolidase with Mn ions and GlyPro ligand

Structural highlights

Disease

Function

References

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