Crystal structure of Escherichia coli UvrB C-terminal domain, and a model for UvrB-uvrC interaction.
A crystal structure of the C-terminal domain of Escherichia coli UvrB (UvrB') has been solved to 3.0 A 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 A.
Sohi
M
M
The Randall Institute, King's College, 26-29 Drury Lane, London, UK.
Alexandrovich
A
A
Moolenaar
G
G
Visse
R
R
Goosen
N
N
Vernede
X
X
Fontecilla-Camps
J C
JC
Champness
J
J
Sanderson
M R
MR
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D018360:Crystallography, X-Ray; D004265:DNA Helicases; D019281:Dimerization; D004706:Endodeoxyribonucleases; D004926:Escherichia coli / Q000737:chemistry*; D029968:Escherichia coli Proteins; D018257:Helix-Loop-Helix Motifs; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C058093:UvrB protein, E coli; D004706:Endodeoxyribonucleases; C066567:UvrC protein, E coli; D004265:DNA Helicases