5c3u
From Proteopedia
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| - | ''' | + | ==Crystal structure of a fungal L-serine ammonia-lyase from Rhizomucor miehei== |
| + | <StructureSection load='5c3u' size='340' side='right' caption='[[5c3u]], [[Resolution|resolution]] 1.76Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5c3u]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C3U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C3U FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-serine_ammonia-lyase L-serine ammonia-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.1.17 4.3.1.17] </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=5c3u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c3u OCA], [http://pdbe.org/5c3u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c3u RCSB], [http://www.ebi.ac.uk/pdbsum/5c3u PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | l-serine ammonia-lyase, as a member of the beta-family of pyridoxal-5'-phosphate (PLP) dependent enzymes, catalyzes the conversion of l-serine (l-threonine) to pyruvate (alpha-ketobutyrate) and ammonia. The crystal structure of l-serine ammonia-lyase from Rhizomucor miehei (RmSDH) was solved at 1.76 A resolution by X-ray diffraction method. The overall structure of RmSDH had the characteristic beta-family PLP dependent enzyme fold. It consisted of two distinct domains, both of which show the typical open twisted alpha/beta structure. A PLP cofactor was located in the crevice between the two domains, which was attached to Lys52 by a Schiff-base linkage. Unique residue substitutions (Gly78, Pro79, Ser146, Ser147 and Thr312) were discovered at the catalytic site of RmSDH by comparison of structures of RmSDH and other reported eukaryotic l-serine ammonia-lyases. Optimal pH and temperature of the purified RmSDH were 7.5 and 40 degrees C, respectively. It was stable in the pH range of 7.0-9.0 and at temperatures below 40 degrees C. This is the first crystal structure of a fungal l-serine ammonia-lyase. It will be useful to study the catalytic mechanism of beta-elimination enzymes and will provide a basis for further enzyme engineering. | ||
| - | + | Crystal structure and characterization of a novel l-serine ammonia-lyase from Rhizomucor miehei.,Qin Z, Yan Q, Ma Q, Jiang Z Biochem Biophys Res Commun. 2015 Oct 23;466(3):431-7. doi:, 10.1016/j.bbrc.2015.09.043. Epub 2015 Sep 11. PMID:26367174<ref>PMID:26367174</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5c3u" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: L-serine ammonia-lyase]] | ||
| + | [[Category: Qiaojuan, Y]] | ||
[[Category: Shaoqing, Y]] | [[Category: Shaoqing, Y]] | ||
[[Category: Zhen, Q]] | [[Category: Zhen, Q]] | ||
| - | [[Category: | + | [[Category: Zhengqiang, J]] |
| + | [[Category: Beta-family plp dependent enzyme]] | ||
| + | [[Category: Lyase]] | ||
Revision as of 13:38, 9 December 2015
Crystal structure of a fungal L-serine ammonia-lyase from Rhizomucor miehei
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