|
type |
Journal Article |
authors |
Palani K, Burley SK, Swaminathan S |
title |
Structure of alanine racemase from Oenococcus oeni with bound pyridoxal 5'-phosphate |
journal |
Acta Crystallogr F Struct Biol Commun |
Activity |
5.1.1.5 |
Family |
5.1.1.5.b |
sel |
selected |
ui |
23295479 |
year |
(2013) |
volume |
69 |
number |
1 |
pages |
15-9 |
| |
keywords |
doi: 10.1107/S1744309112047276 |
abstract |
The crystal structure of alanine racemase from Oenococcus oeni has been determined at 1.7 Å resolution using the single-wavelength anomalous dispersion (SAD) method and selenium-labelled protein. The protein exists as a symmetric dimer in the crystal, with both protomers contributing to the two active sites. Pyridoxal 5'-phosphate, a cofactor, is bound to each monomer and forms a Schiff base with Lys39. Structural comparison of alanine racemase from O. oeni (Alr) with homologous family members revealed similar domain organization and cofactor binding. |
last changed |
2017/12/12 10:17 |
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