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Expression, crystallization and preliminary X-ray crystallographic analysis of cystathionine ?-synthase (XometB) from Xanthomonas oryzae pv. oryzae.

ABSTRACT: Cystathionine ?-synthase (CGS) catalyzes the first step in the transsulfuration pathway leading to the formation of cystathionine from O-succinylhomoserine and L-cysteine through a ?-replacement reaction. As an antibacterial drug target against Xanthomonas oryzae pv. oryzae (Xoo), CGS from Xoo (XometB) was cloned, expressed, purified and crystallized. The XometB crystal diffracted to 2.4?Å resolution and belonged to the tetragonal space group I4(1), with unit-cell parameters a=b=165.4, c=241.7?Å. There were four protomers in the asymmetric unit, with a corresponding solvent content of 73.9%.

SUBMITTER: Ngo HP

PROVIDER: S-EPMC3509977 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature

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Expression, crystallization and preliminary X-ray crystallographic analysis of cystathionine γ-synthase (XometB) from Xanthomonas oryzae pv. oryzae.

Ngo Ho-Phuong-Thuy HP Kim Jin-Kwang JK Kim Seung-Hwan SH Pham Tan-Viet TV Tran Thi-Huyen TH Nguyen Dinh-Duc DD Kim Jeong-Gu JG Chung Sumi S Ahn Yeh-Jin YJ Kang Lin-Woo LW

Acta crystallographica. Section F, Structural biology and crystallization communications 20121114 Pt 12

Cystathionine γ-synthase (CGS) catalyzes the first step in the transsulfuration pathway leading to the formation of cystathionine from O-succinylhomoserine and L-cysteine through a γ-replacement reaction. As an antibacterial drug target against Xanthomonas oryzae pv. oryzae (Xoo), CGS from Xoo (XometB) was cloned, expressed, purified and crystallized. The XometB crystal diffracted to 2.4 Å resolution and belonged to the tetragonal space group I4(1), with unit-cell parameters a=b=165.4, c=241.7 Å ...[more]

PMID: 23192036

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