determination of the crystal structure and active residues of fabv, the enoyl-acp reductase from xanthomonas oryzae测定的晶体结构和活性残留fabv,enoyl-acp还原酶从黄oryzae.pdfVIP

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determination of the crystal structure and active residues of fabv, the enoyl-acp reductase from xanthomonas oryzae测定的晶体结构和活性残留fabv,enoyl-acp还原酶从黄oryzae.pdf

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determination of the crystal structure and active residues of fabv, the enoyl-acp reductase from xanthomonas oryzae测定的晶体结构和活性残留fabv,enoyl-acp还原酶从黄oryzae

Determination of the Crystal Structure and Active Residues of FabV, the Enoyl-ACP Reductase from Xanthomonas oryzae 1. 1,2. 1 2 1 He Li , Xiaoli Zhang , Lijun Bi , Jin He *, Tao Jiang * 1 National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, People’s Republic of China, 2 State Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan, Hubei, People’s Republic of China Abstract Background: Enoyl-ACP reductase (ENR) catalyses the last reduction reaction in the fatty acid elongation cycle in bacteria and is a good antimicrobial target candidate. FabV is the most recently discovered class of ENR, but we lack information about the atomic structure and the key residues involved in reductase activity except for the known conserved tyrosine and lysine residues in the Y-X8-K active site motif. Methodology/Principal Findings: Here we report the crystal structure of FabV from Xanthomonas oryzae (xoFabV). The ˚ crystal structure of this enzyme has been solved to 1.6 A resolution in space group P2 2 2 . The model of xoFabV consists of 1 1 1 one monomer in the asymmetric unit which is composed of 13 a-helices and 11 b-strands, representing a canonical Rossmann fold architecture. Structural comparison presents that the locations of the conserved tyrosine (Y236) and lysine (K245) residues in the Y-X -K active site motif of xoFabV and the Y-X -K motif of ecFabI are notably similar. Howev