This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1csp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 7: Line 7:
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1csp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1csp OCA], [http://www.ebi.ac.uk/pdbsum/1csp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1csp RCSB]</span>
}}
}}
Line 26: Line 29:
[[Category: transcription regulation]]
[[Category: transcription regulation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:28:29 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:27:47 2008''

Revision as of 16:27, 30 March 2008


PDB ID 1csp

Drag the structure with the mouse to rotate
, resolution 2.45Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE BACILLUS SUBTILIS MAJOR COLD SHOCK PROTEIN, CSPB: A UNIVERSAL NUCLEIC-ACID BINDING DOMAIN


Overview

The cold-shock response in both Escherichia coli and Bacillus subtilis is induced by an abrupt downshift in growth temperature. It leads to the increased production of the major cold-shock proteins, CS7.4 and CspB, respectively. CS7.4 is a transcriptional activator of two genes. CS7.4 and CspB share 43 per cent sequence identity with the nucleic acid-binding domain of the eukaryotic gene-regulatory Y-box factors. This cold-shock domain is conserved from bacteria to man and contains the RNA-binding RNP1 sequence motif. As a prototype of the cold-shock domain, the structure of CspB has been determined here from two crystal forms. In both, CspB is present as an antiparallel five-stranded beta-barrel. Three consecutive beta-strands, the central one containing the RNP1 motif, create a surface rich in aromatic and basic residues that are presumably involved in nucleic acid binding. Preferential binding of CspB to single-stranded DNA is observed in gel retardation experiments.

About this Structure

1CSP is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein., Schindelin H, Marahiel MA, Heinemann U, Nature. 1993 Jul 8;364(6433):164-8. PMID:8321288

Page seeded by OCA on Sun Mar 30 19:27:47 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools