7c72: Difference between revisions
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<StructureSection load='7c72' size='340' side='right'caption='[[7c72]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='7c72' size='340' side='right'caption='[[7c72]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7c72]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[7c72]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7C72 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7C72 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.0000446Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLT:D-MALATE'>MLT</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=7c72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c72 OCA], [https://pdbe.org/7c72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7c72 RCSB], [https://www.ebi.ac.uk/pdbsum/7c72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7c72 ProSAT]</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=7c72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c72 OCA], [https://pdbe.org/7c72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7c72 RCSB], [https://www.ebi.ac.uk/pdbsum/7c72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7c72 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Feng | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Jiang | [[Category: Feng Q]] | ||
[[Category: Lukman | [[Category: Jiang J]] | ||
[[Category: Ruiz-Carrillo | [[Category: Lukman M]] | ||
[[Category: Zhang | [[Category: Ruiz-Carrillo D]] | ||
[[Category: Zhao | [[Category: Zhang Y]] | ||
[[Category: Zhou | [[Category: Zhao YH]] | ||
[[Category: Zhou X]] | |||
Latest revision as of 18:58, 29 November 2023
Structure of a mycobacterium tuberculosis puromycin-hydrolyzing peptidaseStructure of a mycobacterium tuberculosis puromycin-hydrolyzing peptidase
Structural highlights
Publication Abstract from PubMedPuromycin-hydrolizing peptidases have been described as members of the prolyl oligopeptidase peptidase family. These enzymes are present across all domains of life but still little is known of the homologs found in the pathogenic bacterium Mycobacterium tuberculosis. The crystal structure of a M. tuberculosis puromycin hydrolase peptidase has been determined at 3 Angstrom resolution, revealing a conserved prolyl oligopeptidase fold, defined by alpha/beta-hydrolase and beta-propeller domains with two distinctive loops that occlude access of large substrates to the active site. The enzyme displayed amino peptidase activity with a substrate specificity preference for hydrophobic residues in the decreasing order of phenylalanine, leucine, alanine and proline. The enzyme's active site is lined by residues Glu564 for the coordination of the substrates amino terminal moiety and His561, Val608, Tyr78, Trp306, Phe563 and Ty567 for the accommodation of hydrophobic substrates. The availability of a crystal structure for puromycin hydrolase of M. tuberculosis shall facilitate the development of inhibitors with therapeutic applications. Mycobacterium tuberculosis puromycin hydrolase displays a prolyl oligopeptidase fold and an acyl aminopeptidase activity.,Zhao Y, Feng Q, Zhou X, Zhang Y, Lukman M, Jiang J, Ruiz-Carrillo D Proteins. 2021 Jan 10. doi: 10.1002/prot.26044. PMID:33426726[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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