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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]

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