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381087 is a member of PF01168, alanine racemase N-term domain. This protein is likely a bacterial homolog of the yeast D-serine dehydratase YGL196W (see reference below). The protein functions as a dimer. It contains a TIM fold at the middle part, the N-term is involved in dimerization, the C-term folds into a separate domain, also near the domain interface.
It is likely that this enzyme functions in D-amino acid metabolism, and binds PLP, based on gene neighborhood and the structure similarity of the middle section with 1xfc. However, the active sites differs significantly, except for Lys78 and Arg275. As a result, further analysis is needed to understand the function of this protein (eg does it really binds PLP, how?).
The closest structural matches by SSM include: 1njj, 3c5q, 2qgh. The active site in the TIM domain (near H76) bears similarity to 1njj, but is not highly conserved.
Need to try co-xtallization with PLP.
Figure 1 monomer
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Figure 2 dimer
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Biochem. J. (2008) 409, 399–406 (Printed in Great Britain) doi:10.1042/BJ20070642