Crystal structure of maize serine racemase with pyridoxal 5′-phosphate
Open Access
- 16 February 2016
- journal article
- research article
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section F Structural Biology Communications
- Vol. 72 (3) , 165-171
Abstract
Serine racemase (SR) is a pyridoxal 5′-phosphate (PLP)-dependent enzyme that is responsible for D-serine biosynthesisin vivo. The first X-ray crystal structure of maize SR was determined to 2.1 Å 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.Keywords
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