1M0V

NMR STRUCTURE OF THE TYPE III SECRETORY DOMAIN OF YERSINIA YOPH COMPLEXED WITH THE SKAP-HOM PHOSPHO-PEPTIDE N-acetyl-DEpYDDPF-NH2

1M0V の概要

• エントリーDOI: 10.2210/pdb1m0v/pdb
• 分子名称: PROTEIN-TYROSINE PHOSPHATASE YOPH, SKAP55 homologue (2 entities in total)
• 機能のキーワード: high resolution structure, hydrolase
• 由来する生物種: Yersinia pseudotuberculosis; 詳細
• 細胞内の位置: Secreted: p08538
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 15886.48

構造登録者

Khandelwal, P.,Keliikuli, K.,Smith, C.L.,Saper, M.A.,Zuiderweg, E.R.P. (登録日: 2002-06-14, 公開日: 2002-07-24, 最終更新日: 2024-11-20)

主引用文献

Khandelwal, P.,Keliikuli, K.,Smith, C.L.,Saper, M.A.,Zuiderweg, E.R.P.
Solution structure and phosphopeptide binding to the N-terminal domain of Yersinia YopH: comparison with a crystal structure
Biochemistry, 41:11425-11437, 2002

PubMed Abstract: Virulence of pathogenic bacteria of the genus Yersinia requires the injection of six effector proteins into the cytoplasm of host cells. The amino-terminal domain of one of these effectors, the tyrosine phosphatase YopH, is essential for translocation of YopH, as well as for targeting it to phosphotyrosine-containing substrates of the type pYxxP. We report the high-resolution solution structure of the N-terminal domain (residues 1-129) from the Yersinia pseudotuberculosis YopH (YopH-NT) in complex with N-acetyl-DEpYDDPF-NH(2), a peptide derived from an in vivo protein substrate. In contrast to the domain-swapped dimer observed in a crystal structure of the same protein (Smith, C. L., Khandelwal, P., Keliikuli, K., Zuiderweg, E. R. P., and Saper, M. A. (2001) Mol. Microbiol. 42, 967-979), YopH-NT is monomeric in solution. The peptide binding site is located on a beta-hairpin that becomes the crossover point in the dimer structure. The binding site has several characteristics that are reminiscent of SH2 domains, which also bind to pYxxP sequences.

PubMed: 12234185
DOI: 10.1021/bi026333l

実験手法

SOLUTION NMR