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Crystal structure of HslUV complexed with a vinyl sulfone inhibitor: corroboration of a proposed mechanism of allosteric activation of HslV by HslU.

Abstract:

On the basis of the structure of a HslUV complex, a mechanism of allosteric activation of the HslV protease, wherein binding of the HslU chaperone propagates a conformational change to the active site cleft of the protease, has been proposed. Here, the 3.1 A X-ray crystallographic structure of Haemophilus influenzae HslUV complexed with a vinyl sulfone inhibitor is described. The inhibitor, which reacts to form a covalent linkage to Thr1 of HslV, binds in an "antiparallel beta" manner, with h...

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Publication status:
Published

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Journal:
Journal of molecular biology
Volume:
318
Issue:
3
Pages:
779-785
Publication date:
2002-05-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:532b3e98-19c0-4496-b3ac-0452d5ddbbf3
Source identifiers:
9118
Local pid:
pubs:9118

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