5mc4: Difference between revisions
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==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=''> | |||
== 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> | |||
</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: | <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: | [[Category: Hydrolase]] | ||
[[Category: | [[Category: Hydrolysis]] | ||
[[Category: Metalloenzyme]] | |||
[[Category: Mutation]] | |||
[[Category: Peptidase]] | |||
[[Category: Pita-bread]] | |||
[[Category: Prolidase]] | |||
