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.


2hax

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2hax.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2hax.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2hax| PDB=2hax | SCENE= }}
{{STRUCTURE_2hax| PDB=2hax | SCENE= }}
-
'''Crystal structure of Bacillus caldolyticus cold shock protein in complex with hexathymidine'''
+
===Crystal structure of Bacillus caldolyticus cold shock protein in complex with hexathymidine===
-
==Overview==
+
<!--
-
Bacterial cold shock proteins (CSPs) regulate cellular adaptation to cold stress. Functions ascribed to CSP include roles as RNA chaperones and in transcription antitermination. We present the crystal structure of the Bacillus caldolyticus CSP (Bc-Csp) in complex with hexathymidine (dT(6)) at a resolution of 1.29 A. Bound to dT(6), crystalline Bc-Csp forms a domain-swapped dimer in which beta strands 1-3 associate with strands 4 and 5 from the other subunit to form a closed beta barrel and vice versa. The globular units of dimeric Bc-Csp closely resemble the well-known structure of monomeric CSP. Structural reorganization from the monomer to the domain-swapped dimer involves a strictly localized change in the peptide bond linking Glu36 and Gly37 of Bc-Csp. Similar structural reorganizations have not been found in any other CSP or oligonucleotide/oligosaccharide-binding fold structures. Each dT(6) ligand is bound to one globular unit of Bc-Csp via an amphipathic protein surface. Individual binding subsites interact with the DNA bases through stacking and hydrogen bonding. The sugar-phosphate backbone remains solvent exposed. Based on crystallographic and biochemical studies of deoxyoligonucleotide binding to CSP, we suggest a common mode of binding of single-stranded heptanucleotide motifs to proteins containing cold shock domains, including the eukaryotic Y-box factors.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17266726}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17266726 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17266726}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Protein-dna complex]]
[[Category: Protein-dna complex]]
[[Category: Single-stranded dna]]
[[Category: Single-stranded dna]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:04:18 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 6 00:58:28 2008''

Revision as of 21:58, 5 July 2008

Image:2hax.png

Template:STRUCTURE 2hax

Crystal structure of Bacillus caldolyticus cold shock protein in complex with hexathymidine

Template:ABSTRACT PUBMED 17266726

About this Structure

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

Reference

Common mode of DNA binding to cold shock domains. Crystal structure of hexathymidine bound to the domain-swapped form of a major cold shock protein from Bacillus caldolyticus., Max KE, Zeeb M, Bienert R, Balbach J, Heinemann U, FEBS J. 2007 Mar;274(5):1265-79. Epub 2007 Jan 31. PMID:17266726

Page seeded by OCA on Sun Jul 6 00:58:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2hax"
Personal tools