3v7z: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='3v7z' size='340' side='right'caption='[[3v7z]], [[Resolution|resolution]] 1.61Å' scene=''> | <StructureSection load='3v7z' size='340' side='right'caption='[[3v7z]], [[Resolution|resolution]] 1.61Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3v7z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3v7z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V7Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V7Z FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GEM:(2-GUANIDINOETHYLMERCAPTO)SUCCINIC+ACID'>GEM</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.61Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GEM:(2-GUANIDINOETHYLMERCAPTO)SUCCINIC+ACID'>GEM</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3v7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v7z OCA], [https://pdbe.org/3v7z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v7z RCSB], [https://www.ebi.ac.uk/pdbsum/3v7z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v7z 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=3v7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v7z OCA], [https://pdbe.org/3v7z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v7z RCSB], [https://www.ebi.ac.uk/pdbsum/3v7z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v7z ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/CBPT_THEVU CBPT_THEVU] Able to split off hydrophobic and basic amino acids with comparable efficiency. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 27: | Line 26: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thermoactinomyces vulgaris]] | ||
[[Category: | [[Category: Akparov VK]] | ||
[[Category: | [[Category: Kuranova IP]] | ||
[[Category: | [[Category: Kuznetsov SA]] | ||
[[Category: | [[Category: Timofeev VI]] | ||
Latest revision as of 13:33, 6 November 2024
Carboxypeptidase T with GEMSACarboxypeptidase T with GEMSA
Structural highlights
FunctionCBPT_THEVU Able to split off hydrophobic and basic amino acids with comparable efficiency. Publication Abstract from PubMedThe crystal structures of carboxypeptidase T (CpT) complexes with phenylalanine and arginine substrate analogs - benzylsuccinic acid and (2-guanidinoethylmercapto)succinic acid - were determined by the molecular replacement method at resolutions of 1.57 A and 1.62 A to clarify the broad substrate specificity profile of the enzyme. The conservative Leu211 and Leu254 residues (also present in both carboxypeptidase A and carboxypeptidase B) were shown to be structural determinants for recognition of hydrophobic substrates, whereas Asp263 was for recognition of positively charged substrates. Mutations of these determinants modify the substrate profile: the CpT variant Leu211Gln acquires carboxypeptidase B-like properties, and the CpT variant Asp263Asn the carboxypeptidase A-like selectivity. The Pro248-Asp258 loop interacting with Leu254 and Tyr255 was shown to be responsible for recognition of the substrate's C-terminal residue. Substrate binding at the S1' subsite leads to the ligand-dependent shift of this loop, and Leu254 side chain movement induces the conformation rearrangement of the Glu277 residue crucial for catalysis. This is a novel insight into the substrate selectivity of metallocarboxypeptidases that demonstrates the importance of interactions between the S1' subsite and the catalytic center. Structural insights into the broad substrate specificity of carboxypeptidase T from Thermoactinomyces vulgaris.,Akparov VKh, Timofeev VI, Khaliullin IG, Svedas V, Chestukhina GG, Kuranova IP FEBS J. 2015 Apr;282(7):1214-24. doi: 10.1111/febs.13210. Epub 2015 Feb 18. PMID:25619204[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||