2es2
From Proteopedia
(New page: 200px<br /><applet load="2es2" size="450" color="white" frame="true" align="right" spinBox="true" caption="2es2, resolution 1.780Å" /> '''Crystal Structure A...) |
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| - | [[Image:2es2.gif|left|200px]]<br /><applet load="2es2" size=" | + | [[Image:2es2.gif|left|200px]]<br /><applet load="2es2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2es2, resolution 1.780Å" /> | caption="2es2, resolution 1.780Å" /> | ||
'''Crystal Structure Analysis of the Bacillus Subtilis Cold Shock Protein Bs-CspB in Complex with Hexathymidine'''<br /> | '''Crystal Structure Analysis of the Bacillus Subtilis Cold Shock Protein Bs-CspB in Complex with Hexathymidine'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Bacterial cold shock proteins (CSPs) are involved in cellular adaptation | + | 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== | ==About this Structure== | ||
| - | 2ES2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2ES2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ES2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bienert, M.]] | [[Category: Bienert, M.]] | ||
[[Category: Heinemann, U.]] | [[Category: Heinemann, U.]] | ||
| - | [[Category: Max, K | + | [[Category: Max, K E.A.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
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[[Category: single-stranded dna]] | [[Category: single-stranded dna]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:13:58 2008'' |
Revision as of 15:13, 21 February 2008
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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 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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