Structure of XC6422 from Xanthomonas campestris at 1.6 Å resolution: A small serine α/β-hydrolase

Chao Yu Yang, Ko Hsin Chin, Chia Cheng Chou, Andrew H.J. Wang, Shan Ho Chou

研究成果: 雜誌貢獻文章同行評審

4 引文 斯高帕斯(Scopus)

摘要

XC6422 is a conserved hypothetical protein from Xanthomonas campestris pathovar campestris (Xcc), a Gram-negative yellow-pigmented pathogenic bacterium that causes black rot, one of the major worldwide diseases of cruciferous crops. The protein consists of 220 amino acids and its structure has been determined to 1.6 Å resolution using the multi-wavelength anomalous dispersion (MAD) method. Although it has very low sequence identity to protein sequences in the PDB (less than 20%), the determined structure nevertheless shows that it belongs to the superfamily of serine α/β-hydrolases, with an active site that is fully accessible to solvent owing to the absence of a lid domain. Modelling studies with the serine esterase inhibitor E600 indicate that XC6422 adopts a conserved Ser-His-Asp catalytic triad common to this superfamily and has a preformed oxyanion hole for catalytic activation. These structural features suggest that XC6422 is most likely to be a hydrolase active on a soluble ester or a small lipid. An extra strand preceding the first β-strand in the canonical α/β-hydrolase fold leads to extensive subunit interactions between XC6422 monomers, which may explain why XC6422 crystals of good diffraction quality can grow to dimensions of up to 1.5 mm in a few days.

原文英語
頁(從 - 到)498-503
頁數6
期刊Acta Crystallographica Section F: Structural Biology and Crystallization Communications
62
發行號6
DOIs
出版狀態已發佈 - 6月 2006
對外發佈

ASJC Scopus subject areas

  • 生物物理學
  • 結構生物學
  • 生物化學
  • 遺傳學
  • 凝聚態物理學

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