6srf
From Proteopedia
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==Crystal Structure of Human Prolidase G278N variant expressed in the presence of chaperones== | ==Crystal Structure of Human Prolidase G278N variant expressed in the presence of chaperones== | ||
| - | <StructureSection load='6srf' size='340' side='right'caption='[[6srf]]' scene=''> | + | <StructureSection load='6srf' size='340' side='right'caption='[[6srf]], [[Resolution|resolution]] 1.85Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SRF OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6srf]] 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=6SRF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SRF FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.847Å</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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></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=6srf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6srf OCA], [https://pdbe.org/6srf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6srf RCSB], [https://www.ebi.ac.uk/pdbsum/6srf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6srf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Disease == | ||
| + | [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 == | ||
| + | [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;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Prolidase catalyzes the cleavage of dipeptides containing proline on their C terminus. The reduction in prolidase activity is the cause of a rare disease named 'Prolidase Deficiency'. Local structural disorder was indicated as one of the causes for diminished prolidase activity. Previous studies showed that heat shock proteins can partially recover prolidase activity in vivo. To analyze this mechanism of enzymatic activity rescue, we compared the crystal structures of selected prolidase mutants expressed in the absence and in the presence of chaperones. Our results confirm that protein chaperones facilitate the formation of more ordered structures by their substrate protein. These results also suggest that the protein expression system needs to be considered as an important parameter in structural studies. DATABASES: The reported crystal structures and their associated structure factor amplitudes were deposited in the Protein Data Bank under the accession codes 6SRE, 6SRF, and 6SRG, respectively. | ||
| + | |||
| + | Co-expression with chaperones can affect protein 3D structure as exemplified by loss-of-function variants of human prolidase.,Wator E, Rutkiewicz M, Weiss MS, Wilk P FEBS Lett. 2020 Sep;594(18):3045-3056. doi: 10.1002/1873-3468.13877. Epub 2020, Jul 14. PMID:32598484<ref>PMID:32598484</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6srf" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Wator E]] | [[Category: Wator E]] | ||
[[Category: Wilk P]] | [[Category: Wilk P]] | ||
Revision as of 12:46, 24 January 2024
Crystal Structure of Human Prolidase G278N variant expressed in the presence of chaperones
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