5ell
From Proteopedia
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(New page: ==Crystal structure of L-aspartate/glutamate-specific racemase from Escherichia coli== <StructureSection load='5ell' size='340' side='right' caption='5ell, resolution 1....) |
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==Crystal structure of L-aspartate/glutamate-specific racemase from Escherichia coli== | ==Crystal structure of L-aspartate/glutamate-specific racemase from Escherichia coli== | ||
| - | <StructureSection load='5ell' size='340' side='right' caption='[[5ell]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='5ell' size='340' side='right'caption='[[5ell]], [[Resolution|resolution]] 1.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5ell]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ELL OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5ell]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ELL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ELL 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]] 1.801Å</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=5ell FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ell OCA], [https://pdbe.org/5ell PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ell RCSB], [https://www.ebi.ac.uk/pdbsum/5ell PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ell ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/C3SWD2_ECOLX C3SWD2_ECOLX] | ||
| + | <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. | ||
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| + | 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> | ||
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| + | From MEDLINE®/PubMed®, 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__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Ahn JW]] |
| - | [[Category: | + | [[Category: Chang JH]] |
| - | [[Category: | + | [[Category: Kim KJ]] |
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Current revision
Crystal structure of L-aspartate/glutamate-specific racemase from Escherichia coli
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