5ell: Difference between revisions

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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=5ell FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ell OCA], [http://pdbe.org/5ell PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ell RCSB], [http://www.ebi.ac.uk/pdbsum/5ell PDBsum]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

We determined the crystal structure of EcL-DER to elucidate protein function and substrate specificity. Unlike other asp/glu racemases, EcL-DER has an unbalanced pair of catalytic residues, Thr83/Cys197, at the active site that is crucial for l- to d-unidirectional racemase activity. EcL-DER exhibited racemase activity for both l-glutamate and l-aspartate, but had threefold higher activity for l-glutamate. Based on the structure of the EcL-DER(C197S) mutant in complex with l-glutamate, we determined the binding mode of the l-glutamate substrate in EcL-DER and provide a structural basis for how the protein utilizes l-glutamate as a main substrate. The unidirectionality, despite an equilibrium constant of unity, can be understood in terms of the Haldane relationship.

Structural basis for an atypical active site of an l-aspartate/glutamate-specific racemase from Escherichia coli.,Ahn JW, Chang JH, Kim KJ FEBS Lett. 2015 Dec 21;589(24 Pt B):3842-7. doi: 10.1016/j.febslet.2015.11.003., Epub 2015 Nov 7. PMID:26555188<ref>PMID:26555188</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

__TOC__

</StructureSection>

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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=5ell FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ell OCA], [http://pdbe.org/5ell PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ell RCSB], [http://www.ebi.ac.uk/pdbsum/5ell PDBsum]</span></td></tr>
 </table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+We determined the crystal structure of EcL-DER to elucidate protein function and substrate specificity. Unlike other asp/glu racemases, EcL-DER has an unbalanced pair of catalytic residues, Thr83/Cys197, at the active site that is crucial for l- to d-unidirectional racemase activity. EcL-DER exhibited racemase activity for both l-glutamate and l-aspartate, but had threefold higher activity for l-glutamate. Based on the structure of the EcL-DER(C197S) mutant in complex with l-glutamate, we determined the binding mode of the l-glutamate substrate in EcL-DER and provide a structural basis for how the protein utilizes l-glutamate as a main substrate. The unidirectionality, despite an equilibrium constant of unity, can be understood in terms of the Haldane relationship.
+Structural basis for an atypical active site of an l-aspartate/glutamate-specific racemase from Escherichia coli.,Ahn JW, Chang JH, Kim KJ FEBS Lett. 2015 Dec 21;589(24 Pt B):3842-7. doi: 10.1016/j.febslet.2015.11.003., Epub 2015 Nov 7. PMID:26555188<ref>PMID:26555188</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 5ell" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>