5CVC

Structure of maize serine racemase

Summary for 5CVC

• Entry DOI: 10.2210/pdb5cvc/pdb
• Descriptor: Serine racemase, MAGNESIUM ION, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total)
• Functional Keywords: maize serine racemase, isomerase
• Biological source: Zea mays (Maize)
• Total number of polymer chains: 3
• Total formula weight: 111063.73

Authors

Song, Y.,Zou, L.,Fan, J. (deposition date: 2015-07-26, release date: 2016-03-16, Last modification date: 2023-11-08)

Primary citation

Zou, L.,Song, Y.,Wang, C.,Sun, J.,Wang, L.,Cheng, B.,Fan, J.
Crystal structure of maize serine racemase with pyridoxal 5'-phosphate.
Acta Crystallogr.,Sect.F, 72:165-171, 2016

PubMed Abstract: 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 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.

PubMed: 26919519
DOI: 10.1107/S2053230X16000960

Experimental method

X-RAY DIFFRACTION (2.09 Å)