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2es2
From Proteopedia
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| , resolution 1.780Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | cspB, cspA (Bacillus subtilis) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure Analysis of the Bacillus Subtilis Cold Shock Protein Bs-CspB in Complex with Hexathymidine
Overview
Bacterial cold shock proteins (CSPs) are involved in cellular adaptation to cold stress. They bind to single-stranded nucleic acids with a KD value in the micro- to nanomolar range. Here we present the structure of the Bacillus subtilis CspB (Bs-CspB) in complex with hexathymidine (dT6) at a resolution of 1.78 A. Bs-CspB binds to dT6 with nanomolar affinity via an amphipathic interface on the protein surface. Individual binding subsites interact with single nucleobases through stacking interactions and hydrogen bonding. The sugar-phosphate backbone and the methyl groups of the thymine nucleobases remain solvent exposed and are not contacted by protein groups. Fluorescence titration experiments monitoring the binding of oligopyrimidines to Bs-CspB reveal binding preferences at individual subsites and allow the design of an optimised heptapyrimidine ligand, which is bound with sub-nanomolar affinity. This study reveals the stoichiometry and sequence determinants of the binding of single-stranded nucleic acids to a preformed site on Bs-CspB and thus provides the structural basis of the RNA chaperone and transcription antitermination activities of the CSP.
About this Structure
2ES2 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
T-rich DNA single strands bind to a preformed site on the bacterial cold shock protein Bs-CspB., Max KE, Zeeb M, Bienert R, Balbach J, Heinemann U, J Mol Biol. 2006 Jul 14;360(3):702-14. Epub 2006 Jun 2. PMID:16780871
Page seeded by OCA on Thu Mar 20 16:43:41 2008
