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2es2

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|PDB= 2es2 |SIZE=350|CAPTION= <scene name='initialview01'>2es2</scene>, resolution 1.780&Aring;
|PDB= 2es2 |SIZE=350|CAPTION= <scene name='initialview01'>2es2</scene>, resolution 1.780&Aring;
|SITE=
|SITE=
-
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DT:THYMIDINE-5&#39;-MONOPHOSPHATE'>DT</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= cspB, cspA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
|GENE= cspB, cspA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
 +
|DOMAIN=
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|RELATEDENTRY=[[1csp|1CSP]], [[1csq|1CSQ]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2es2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2es2 OCA], [http://www.ebi.ac.uk/pdbsum/2es2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2es2 RCSB]</span>
}}
}}
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[[Category: Heinemann, U.]]
[[Category: Heinemann, U.]]
[[Category: Max, K E.A.]]
[[Category: Max, K E.A.]]
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[[Category: CA]]
 
[[Category: beta barrel]]
[[Category: beta barrel]]
[[Category: protein-dna complex]]
[[Category: protein-dna complex]]
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[[Category: single-stranded dna]]
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[[Category: single-stranded dna,]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:43:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:53:00 2008''

Revision as of 23:53, 30 March 2008


PDB ID 2es2

Drag the structure with the mouse to rotate
, resolution 1.780Å
Ligands: ,
Gene: cspB, cspA (Bacillus subtilis)
Related: 1CSP, 1CSQ


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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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