5cvc
From Proteopedia
Structure of maize serine racemase
Structural highlights
FunctionPublication Abstract from PubMedSerine 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Large Structures | Zea mays | Fan J | Song Y | Zou L
