Crystal structure of Escherichia coli UvrB C‐terminal domain, and a model for UvrB‐UvrC interaction

FEBS Letters

Alexandrovich, Alexander³  Sohi, Maninder³  Moolenaar, Geri¹  Fontecilla-Camps, Juan C.²  Visse, Rob¹  Vernede, Xavier²  Sanderson, Mark R.³  Goosen, Nora¹  Champness, John³ 

[1] Molecular Genetics, Leiden Institute of Chemistry Gorlaeus Laboratories, Leiden Univerisity, Postbus 9502, 2300 RA Leiden, The Netherlands;CEA, CNRS, Institut de Biologie Structurale Jean-Pierre Ebel, Laboratoire de Cristallographie et Cristallogenese, F-38027 Grenoble 1, France;The Randall Institute, King's College, 26–29 Drury Lane, London WC2B 5RL, UK

关键词: Nucleotide excision repair;    X-ray crystallography;    UvrB protein;    UvrB-C interaction;    NMR;    nuclear magnetic resonance;    MAD;    multiple anomalous dispersion;   

DOI  :  10.1016/S0014-5793(99)01690-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A crystal structure of the C-terminal domain of Escherichia coli UvrB (UvrB′) has been solved to 3.0 Å resolution. The domain adopts a helix-loop-helix fold which is stabilised by the packing of hydrophobic side-chains between helices. From the UvrB′ fold, a model for a domain of UvrC (UvrC′) that has high sequence homology with UvrB′ has been made. In the crystal, a dimerisation of UvrB′ domains is seen involving specific hydrophobic and salt bridge interactions between residues in and close to the loop region of the domain. It is proposed that a homologous mode of interaction may occur between UvrB and UvrC. This interaction is likely to be flexible, potentially spanning >50 Å.

【 授权许可】

Unknown