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| | <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 with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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 [http://proteopedia.org/fgij/fg.htm?mol=5ELL FirstGlance]. <br> | + | <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5elm|5elm]]</td></tr> | + | </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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_racemase Aspartate racemase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.1.13 5.1.1.13] </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=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'>[http://proteopedia.org/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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ell ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/C3SWD2_ECOLX C3SWD2_ECOLX] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Aspartate racemase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ahn, J W]] | + | [[Category: Ahn JW]] |
| - | [[Category: Chang, J H]] | + | [[Category: Chang JH]] |
| - | [[Category: Kim, K J]] | + | [[Category: Kim KJ]] |
| - | [[Category: Amino acid enantiomer]]
| + | |
| - | [[Category: Asp/glu racemase]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: L-form specific racemase]]
| + | |
| Structural highlights
Function
C3SWD2_ECOLX
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ahn JW, Chang JH, Kim KJ. Structural basis for an atypical active site of an l-aspartate/glutamate-specific racemase from Escherichia coli. 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 doi:http://dx.doi.org/10.1016/j.febslet.2015.11.003
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