2f52: Difference between revisions
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'''Solution structure of cold shock protein CspB from Bacillus subtilis in complex with heptathymidine''' | {{Structure | ||
|PDB= 2f52 |SIZE=350|CAPTION= <scene name='initialview01'>2f52</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= cspB, cspA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | |||
}} | |||
'''Solution structure of cold shock protein CspB from Bacillus subtilis in complex with heptathymidine''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2F52 is a [ | 2F52 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F52 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16956971 16956971] | ||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ob-fold]] | [[Category: ob-fold]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:48:10 2008'' | ||
Revision as of 14:48, 20 March 2008
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| 2f52 | |||||||||||||
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| Gene: | cspB, cspA (Bacillus subtilis) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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