6a4r

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'''Unreleased structure'''
 
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The entry 6a4r is ON HOLD until Paper Publication
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==Crystal structure of aspartate bound peptidase E from Salmonella enterica==
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<StructureSection load='6a4r' size='340' side='right' caption='[[6a4r]], [[Resolution|resolution]] 1.83&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6a4r]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A4R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A4R FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fy2|1fy2]]</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dipeptidase_E Dipeptidase E], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.13.21 3.4.13.21] </span></td></tr>
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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=6a4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a4r OCA], [http://pdbe.org/6a4r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a4r RCSB], [http://www.ebi.ac.uk/pdbsum/6a4r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a4r ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/PEPE_SALTY PEPE_SALTY]] Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.[HAMAP-Rule:MF_00510]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Peptidase-E, a nonclassical serine peptidase, is specific for dipeptides with an N-terminal aspartate. This stringent substrate specificity remains largely unexplained. We report an aspartate-bound structure of peptidase-E at 1.83 A resolution. In contrast to previous reports, the enzyme forms a dimer, and the active site is located at the dimer interface, well shielded from the solvent. Our findings further suggest that the stringent aspartate specificity of the enzyme is due to electrostatics and molecular complementarity in the active site. The new structural information presented herein may provide insights into the role of functionally important residues in peptidase-E.
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Authors: Yadav, P., Chandravanshi, K., Goyal, V.D., Singh, R., Kumar, A., Gokhale, S.M., Makde, R.D.
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Structure of Asp-bound peptidase E from Salmonella enterica: Active site at dimer interface illuminates Asp recognition.,Yadav P, Goyal VD, Gaur NK, Kumar A, Gokhale SM, Makde RD FEBS Lett. 2018 Oct;592(19):3346-3354. doi: 10.1002/1873-3468.13247. Epub 2018, Sep 21. PMID:30194851<ref>PMID:30194851</ref>
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Description: Crystal structure of aspartate bound peptidase E from Salmonella enterica
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Makde, R.D]]
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<div class="pdbe-citations 6a4r" style="background-color:#fffaf0;"></div>
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[[Category: Gokhale, S.M]]
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== References ==
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[[Category: Goyal, V.D]]
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<references/>
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[[Category: Kumar, A]]
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__TOC__
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</StructureSection>
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[[Category: Dipeptidase E]]
[[Category: Chandravanshi, K]]
[[Category: Chandravanshi, K]]
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[[Category: Gokhale, S M]]
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[[Category: Goyal, V D]]
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[[Category: Kumar, A]]
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[[Category: Makde, R D]]
[[Category: Singh, R]]
[[Category: Singh, R]]
[[Category: Yadav, P]]
[[Category: Yadav, P]]
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[[Category: Active site]]
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[[Category: Active site loop]]
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[[Category: Dimer]]
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[[Category: Hydrolase]]
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[[Category: Peptidase e]]
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[[Category: S51 peptidase]]

Revision as of 05:49, 24 October 2018

Crystal structure of aspartate bound peptidase E from Salmonella enterica

6a4r, resolution 1.83Å

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