4f8z
From Proteopedia
(Difference between revisions)
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<StructureSection load='4f8z' size='340' side='right' caption='[[4f8z]], [[Resolution|resolution]] 1.38Å' scene=''> | <StructureSection load='4f8z' size='340' side='right' caption='[[4f8z]], [[Resolution|resolution]] 1.38Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4f8z]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[4f8z]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43649 Atcc 43649]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F8Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F8Z FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BL2:N-(TERT-BUTOXYCARBONYL)-L-LEUCINE'>BL2</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BL2:N-(TERT-BUTOXYCARBONYL)-L-LEUCINE'>BL2</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cpt ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2026 | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cpt ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2026 ATCC 43649])</td></tr> |
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carboxypeptidase_T Carboxypeptidase T], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.18 3.4.17.18] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carboxypeptidase_T Carboxypeptidase T], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.18 3.4.17.18] </span></td></tr> | ||
| - | <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=4f8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f8z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f8z RCSB], [http://www.ebi.ac.uk/pdbsum/4f8z PDBsum]</span></td></tr> | + | <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=4f8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f8z OCA], [http://pdbe.org/4f8z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4f8z RCSB], [http://www.ebi.ac.uk/pdbsum/4f8z PDBsum]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/CBPT_THEVU CBPT_THEVU]] Able to split off hydrophobic and basic amino acids with comparable efficiency. | [[http://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;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The 3D structure of recombinant bacterial carboxypeptidase T (CPT) in complex with N-BOC-L-leucine was determined at 1.38 A resolution. Crystals for the X-ray study were grown in microgravity using the counter-diffusion technique. N-BOC-L-leucine and SO4(2-) ion bound in the enzyme active site were localized in the electron density map. Location of the leucine side chain in CPT-N-BOC-L-leucine complex allowed identification of the S1 subsite of the enzyme, and its structure was determined. Superposition of the structures of CPT-N-BOC-L-leucine complex and complexes of pancreatic carboxypeptidases A and B with substrate and inhibitors was carried out, and similarity of the S1 subsites in these three carboxypeptidases was revealed. It was found that SO4(2-) ion occupies the same position in the S1' subsite as the C-terminal carboxy group of the substrate. | ||
| + | |||
| + | Three-dimensional structure of carboxypeptidase T from Thermoactinomyces vulgaris in complex with N-BOC-L-leucine.,Timofeev VI, Kuznetsov SA, Akparov VKh, Chestukhina GG, Kuranova IP Biochemistry (Mosc). 2013 Mar;78(3):252-9. doi: 10.1134/S0006297913030061. PMID:23586718<ref>PMID:23586718</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4f8z" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Carboxypeptidase|Carboxypeptidase]] | *[[Carboxypeptidase|Carboxypeptidase]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Atcc 43649]] | ||
[[Category: Carboxypeptidase T]] | [[Category: Carboxypeptidase T]] | ||
| - | [[Category: Thermoactinomyces vulgaris]] | ||
[[Category: Akparov, V K]] | [[Category: Akparov, V K]] | ||
[[Category: Kuranova, I P]] | [[Category: Kuranova, I P]] | ||
Revision as of 06:50, 30 September 2015
Carboxypeptidase T with Boc-Leu
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