2F52

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

2F52 の概要

• エントリーDOI: 10.2210/pdb2f52/pdb
• 関連するPDBエントリー: 1CSP 1NMF
• 分子名称: Cold shock protein cspB (1 entity in total)
• 機能のキーワード: beta barrel, ob-fold, dna binding protein-transcription complex, dna binding protein/transcription
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Cytoplasm: P32081
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7372.13

構造登録者

Zeeb, M.,Sticht, H.,Balbach, J. (登録日: 2005-11-25, 公開日: 2006-09-19, 最終更新日: 2024-05-29)

主引用文献

Zeeb, 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

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

実験手法

SOLUTION NMR