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2F52

Solution structure of cold shock protein CspB from Bacillus subtilis in complex with heptathymidine

Summary for 2F52
Entry DOI10.2210/pdb2f52/pdb
Related1CSP 1NMF
DescriptorCold shock protein cspB (1 entity in total)
Functional Keywordsbeta barrel, ob-fold, dna binding protein-transcription complex, dna binding protein/transcription
Biological sourceBacillus subtilis
Cellular locationCytoplasm: P32081
Total number of polymer chains1
Total formula weight7372.13
Authors
Zeeb, M.,Sticht, H.,Balbach, J. (deposition date: 2005-11-25, release date: 2006-09-19, Last modification date: 2024-05-29)
Primary citationZeeb, M.,Max, K.E.,Weininger, U.,Low, C.,Sticht, H.,Balbach, J.
Recognition of T-rich single-stranded DNA by the cold shock protein Bs-CspB in solution.
Nucleic Acids Res., 34:4561-4571, 2006
Cited by
PubMed Abstract: Cold shock proteins (CSP) belong to the family of single-stranded nucleic acid binding proteins with OB-fold. CSP are believed to function as 'RNA chaperones' and during anti-termination. We determined the solution structure of Bs-CspB bound to the single-stranded DNA (ssDNA) fragment heptathymidine (dT7) by NMR spectroscopy. Bs-CspB reveals an almost invariant conformation when bound to dT7 with only minor reorientations in loop beta1-beta2 and beta3-beta4 and of few aromatic side chains involved in base stacking. Binding studies of protein variants and mutated ssDNA demonstrated that Bs-CspB associates with ssDNA at almost diffusion controlled rates and low sequence specificity consistent with its biological function. A variation of the ssDNA affinity is accomplished solely by changes of the dissociation rate. 15N NMR relaxation and H/D exchange experiments revealed that binding of dT7 increases the stability of Bs-CspB and reduces the sub-nanosecond dynamics of the entire protein and especially of loop beta3-beta4.
PubMed: 16956971
DOI: 10.1093/nar/gkl376
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

239803

数据于2025-08-06公开中

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