NMR Solution Structure of the 21 kDa Chaperone Protein DnaK Substrate Binding Domain: A Preview of Chaperone-Protein Interaction
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- 作者：Hong Wang ; Alexander V. Kurochkin ; Yuxi Pang ; Weidong Hu ; Gregory C. Flynn ; and Erik R. P. Zuiderweg
- 刊名：Biochemistry
- 出版年：1998
- 出版时间：June 2, 1998
- 年：1998
- 卷：37
- 期：22
- 页码：7929 - 7940
- 全文大小：250K
- 年卷期：v.37,no.22(June 2, 1998)
- ISSN：1520-4995
文摘
The solution structure of the 21 kDa substrate-binding domain ofthe Escherichia coli Hsp70-chaperone protein DnaK (DnaK 386-561) has been determined to aprecision of 1.00 Å (backbone of the
chars/beta2.gif" BORDER=0 ALIGN="middle">-domain) from 1075 experimental restraints obtained frommultinuclear, multidimensional NMRexperiments. The domain is observed to bind to its own C-terminusand offers a preview of the interactionof this chaperone with other proteins. The bound protein region istightly held at a single amino acidposition (a leucyl residue) that is buried in a deep pocket lined withconserved hydrophobic residues. Asecond hydrophobic binding site was identified using paramagneticallylabeled peptides. It is located ina region close to the N-terminus of the domain and may constitute theallosteric region that links substrate-binding affinity with nucleotide binding in the Hsp70chaperones.
chars/beta2.gif" BORDER=0 ALIGN="middle">-domain) from 1075 experimental restraints obtained frommultinuclear, multidimensional NMRexperiments. The domain is observed to bind to its own C-terminusand offers a preview of the interactionof this chaperone with other proteins. The bound protein region istightly held at a single amino acidposition (a leucyl residue) that is buried in a deep pocket lined withconserved hydrophobic residues. Asecond hydrophobic binding site was identified using paramagneticallylabeled peptides. It is located ina region close to the N-terminus of the domain and may constitute theallosteric region that links substrate-binding affinity with nucleotide binding in the Hsp70chaperones.