5cvc: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| (4 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==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: Fan | <div class="pdbe-citations 5cvc" style="background-color:#fffaf0;"></div> | ||
[[Category: Song | == References == | ||
[[Category: Zou | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Zea mays]] | |||
[[Category: Fan J]] | |||
[[Category: Song Y]] | |||
[[Category: Zou L]] | |||
Latest revision as of 16:12, 8 November 2023
Structure of maize serine racemase
| ||||||||||||