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| | <StructureSection load='5c3u' size='340' side='right'caption='[[5c3u]], [[Resolution|resolution]] 1.76Å' scene=''> | | <StructureSection load='5c3u' size='340' side='right'caption='[[5c3u]], [[Resolution|resolution]] 1.76Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5c3u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhizomucor_miehei_cau432 Rhizomucor miehei cau432]. 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> | + | <table><tr><td colspan='2'>[[5c3u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizomucor_miehei_CAU432 Rhizomucor miehei CAU432]. 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 [https://proteopedia.org/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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.76Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c3u ProSAT]</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=5c3u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c3u OCA], [https://pdbe.org/5c3u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c3u RCSB], [https://www.ebi.ac.uk/pdbsum/5c3u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c3u ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0X1KHE6_RHIMI A0A0X1KHE6_RHIMI] |
| | <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: L-serine ammonia-lyase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Rhizomucor miehei cau432]] | + | [[Category: Rhizomucor miehei CAU432]] |
| - | [[Category: Qiaojuan, Y]] | + | [[Category: Qiaojuan Y]] |
| - | [[Category: Shaoqing, Y]] | + | [[Category: Shaoqing Y]] |
| - | [[Category: Zhen, Q]] | + | [[Category: Zhen Q]] |
| - | [[Category: Zhengqiang, J]] | + | [[Category: Zhengqiang J]] |
| - | [[Category: Beta-family plp dependent enzyme]]
| + | |
| - | [[Category: Lyase]]
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| Structural highlights
Function
A0A0X1KHE6_RHIMI
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Qin Z, Yan Q, Ma Q, Jiang Z. Crystal structure and characterization of a novel l-serine ammonia-lyase from Rhizomucor miehei. 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 doi:http://dx.doi.org/10.1016/j.bbrc.2015.09.043
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