2es2

From Proteopedia

Revision as of 07:59, 21 November 2007

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 with CA as ligand. 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

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