2f52

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[[Image:2f52.jpg|left|200px]]
[[Image:2f52.jpg|left|200px]]
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{{Structure
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|PDB= 2f52 |SIZE=350|CAPTION= <scene name='initialview01'>2f52</scene>
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The line below this paragraph, containing "STRUCTURE_2f52", creates the "Structure Box" on the page.
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|GENE= cspB, cspA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
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{{STRUCTURE_2f52| PDB=2f52 | SCENE= }}
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|RELATEDENTRY=[[1csp|1CSP]], [[1nmf|1NMF]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f52 OCA], [http://www.ebi.ac.uk/pdbsum/2f52 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f52 RCSB]</span>
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'''Solution structure of cold shock protein CspB from Bacillus subtilis in complex with heptathymidine'''
'''Solution structure of cold shock protein CspB from Bacillus subtilis in complex with heptathymidine'''
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[[Category: Sticht, H.]]
[[Category: Sticht, H.]]
[[Category: Zeeb, M.]]
[[Category: Zeeb, M.]]
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[[Category: beta barrel]]
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[[Category: Beta barrel]]
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[[Category: ob-fold]]
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[[Category: Ob-fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:28:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:58:07 2008''
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Revision as of 00:28, 4 May 2008

Template:STRUCTURE 2f52

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


Overview

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.

About this Structure

2F52 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Recognition of T-rich single-stranded DNA by the cold shock protein Bs-CspB in solution., Zeeb M, Max KE, Weininger U, Low C, Sticht H, Balbach J, Nucleic Acids Res. 2006;34(16):4561-71. Epub 2006 Sep 6. PMID:16956971 Page seeded by OCA on Sun May 4 03:28:08 2008

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