5cvc
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Structure of maize serine racemase== | |
+ | <StructureSection load='5cvc' size='340' side='right'caption='[[5cvc]], [[Resolution|resolution]] 2.09Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[5cvc]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CVC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CVC FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.09Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=5cvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cvc OCA], [https://pdbe.org/5cvc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cvc RCSB], [https://www.ebi.ac.uk/pdbsum/5cvc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cvc ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/F5CAQ9_MAIZE F5CAQ9_MAIZE] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Serine racemase (SR) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that is responsible for D-serine biosynthesis in vivo. The first X-ray crystal structure of maize SR was determined to 2.1 A resolution and PLP binding was confirmed in solution by UV-Vis absorption spectrometry. Maize SR belongs to the type II PLP-dependent enzymes and differs from the SR of a vancomycin-resistant bacterium. The PLP is bound to each monomer by forming a Schiff base with Lys67. Structural comparison with rat and fission yeast SRs reveals a similar arrangement of active-site residues but a different orientation of the C-terminal helix. | ||
- | + | Crystal structure of maize serine racemase with pyridoxal 5'-phosphate.,Zou L, Song Y, Wang C, Sun J, Wang L, Cheng B, Fan J Acta Crystallogr F Struct Biol Commun. 2016 Mar 1;72(Pt 3):165-71. doi:, 10.1107/S2053230X16000960. Epub 2016 Feb 16. PMID:26919519<ref>PMID:26919519</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
- | [[Category: | + | <div class="pdbe-citations 5cvc" style="background-color:#fffaf0;"></div> |
- | [[Category: Fan | + | == References == |
- | [[Category: Song | + | <references/> |
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Zea mays]] | ||
+ | [[Category: Fan J]] | ||
+ | [[Category: Song Y]] | ||
+ | [[Category: Zou L]] |
Current revision
Structure of maize serine racemase
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Categories: Large Structures | Zea mays | Fan J | Song Y | Zou L