1qoj

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|PDB= 1qoj |SIZE=350|CAPTION= <scene name='initialview01'>1qoj</scene>, resolution 3.0&Aring;
|PDB= 1qoj |SIZE=350|CAPTION= <scene name='initialview01'>1qoj</scene>, resolution 3.0&Aring;
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qoj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qoj OCA], [http://www.ebi.ac.uk/pdbsum/1qoj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qoj RCSB]</span>
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[[Category: x-ray crystallography]]
[[Category: x-ray crystallography]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:40:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:16:43 2008''

Revision as of 20:16, 30 March 2008


PDB ID 1qoj

Drag the structure with the mouse to rotate
, resolution 3.0Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF E.COLI UVRB C-TERMINAL DOMAIN, AND A MODEL FOR UVRB-UVRC INTERACTION.


Overview

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.

About this Structure

1QOJ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of Escherichia coli UvrB C-terminal domain, and a model for UvrB-uvrC interaction., Sohi M, Alexandrovich A, Moolenaar G, Visse R, Goosen N, Vernede X, Fontecilla-Camps JC, Champness J, Sanderson MR, FEBS Lett. 2000 Jan 14;465(2-3):161-4. PMID:10631326

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