|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6jym' size='340' side='right'caption='[[6jym]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='6jym' size='340' side='right'caption='[[6jym]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6jym]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Haldh Haldh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JYM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6JYM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6jym]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haliotis_discus_hannai Haliotis discus hannai]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JYM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JYM FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PREP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=42344 HALDH])</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]] 1.5Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_oligopeptidase Prolyl oligopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.26 3.4.21.26] </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=6jym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jym OCA], [https://pdbe.org/6jym PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jym RCSB], [https://www.ebi.ac.uk/pdbsum/6jym PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jym 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=6jym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jym OCA], [http://pdbe.org/6jym PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jym RCSB], [http://www.ebi.ac.uk/pdbsum/6jym PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jym ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A1X9T5X9_HALDH A0A1X9T5X9_HALDH] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 24: |
Line 25: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Haldh]] | + | [[Category: Haliotis discus hannai]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Prolyl oligopeptidase]]
| + | [[Category: Cao M]] |
| - | [[Category: Cao, M]] | + | [[Category: Jin T]] |
| - | [[Category: Jin, T]] | + | [[Category: Li W]] |
| - | [[Category: Li, W]] | + | |
| - | [[Category: A serine protease subfamily]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
A0A1X9T5X9_HALDH
Publication Abstract from PubMed
Aimed to study the characteristics of prolyl endopeptidase (PEP, EC 3.4.21.26) and its possible role in the degradation of collagen, we cloned the full-length cDNA sequence of PEP from abalone (Haliotis discus hannai) (Hdh-PEP). Recombinant Hdh-PEP (rHdh-PEP) was expressed in vitro, its enzymatic properties were detected, and its secondary structure was analyzed by Circular Dichroism (CD). We for the first time determined the 1.5 A crystal structure of rHdh-PEP. The decomposition effect of rHdh-PEP on collagen peptides was analyzed. Our data revealed that the molecular weight of rHdh-PEP is 85 kDa, consisting of a catalytic domain and a beta-propeller domain. The optimal pH and temperature of rHdh-PEP were pH 6.0 and 20 degrees C, respectively. Using small collagen peptides as substrates, HPLC-ESI-MS analysis confirmed that rHdh-PEP specifically cleaved at the carboxyl side of proline residues, suggesting its role in the degradation of collagen peptides during autolysis.
Characterization and crystal structure of prolyl endopeptidase from abalone (Haliotis discus hannai).,Li WY, Li Y, Chen YL, Hu JJ, Mengist HM, Liu GM, Jin T, Cao MJ Food Chem. 2020 Dec 15;333:127452. doi: 10.1016/j.foodchem.2020.127452. Epub 2020, Jul 4. PMID:32673951[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li WY, Li Y, Chen YL, Hu JJ, Mengist HM, Liu GM, Jin T, Cao MJ. Characterization and crystal structure of prolyl endopeptidase from abalone (Haliotis discus hannai). Food Chem. 2020 Dec 15;333:127452. doi: 10.1016/j.foodchem.2020.127452. Epub 2020, Jul 4. PMID:32673951 doi:http://dx.doi.org/10.1016/j.foodchem.2020.127452
|
