5t88: Difference between revisions

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 ==Prolyl oligopeptidase from Pyrococcus furiosus==
-<StructureSection load='5t88' size='340' side='right' caption='[[5t88]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+<StructureSection load='5t88' size='340' side='right'caption='[[5t88]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[5t88]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43587 Atcc 43587]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T88 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T88 FirstGlance]. <br>
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 <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=5t88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t88 OCA], [http://pdbe.org/5t88 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t88 RCSB], [http://www.ebi.ac.uk/pdbsum/5t88 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t88 ProSAT]</span></td></tr>
 </table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Enzymes in the prolyl oligopeptidase family possess unique structures and substrate specificities that are important for their biological activity and for potential biocatalytic applications. The crystal structures of Pyrococcus furiosus ( Pfu) prolyl oligopeptidase (POP) and the corresponding S477C mutant were determined to 1.9 and 2.2 A resolution, respectively. The wild type enzyme crystallized in an open conformation, indicating that this state is readily accessible, and it contained bound chloride ions and a prolylproline ligand. These structures were used as starting points for molecular dynamics simulations of Pfu POP conformational dynamics. The simulations showed that large-scale domain opening and closing occurred spontaneously, providing facile substrate access to the active site. Movement of the loop containing the catalytically essential histidine into a conformation similar to those found in structures with fully formed catalytic triads also occurred. This movement was modulated by chloride binding, providing a rationale for experimentally observed activation of POP peptidase catalysis by chloride. Thus, the structures and simulations reported in this study, combined with existing biochemical data, provide a number of insights into POP catalysis.
+Crystal Structure and Conformational Dynamics of Pyrococcus furiosus Prolyl Oligopeptidase.,Ellis-Guardiola K, Rui H, Beckner RL, Srivastava P, Sukumar N, Roux B, Lewis JC Biochemistry. 2019 Mar 26;58(12):1616-1626. doi: 10.1021/acs.biochem.9b00031., Epub 2019 Mar 5. PMID:30786206<ref>PMID:30786206</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 5t88" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Prolyl Endopeptidase|Prolyl Endopeptidase]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>
 [[Category: Atcc 43587]]
+[[Category: Large Structures]]
 [[Category: Ellis-Guardiola, K]]
 [[Category: Lewis, J]]