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1r63

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[[Image:1r63.gif|left|200px]]
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{{STRUCTURE_1r63| PDB=1r63 | SCENE= }}
{{STRUCTURE_1r63| PDB=1r63 | SCENE= }}
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'''STRUCTURAL ROLE OF A BURIED SALT BRIDGE IN THE 434 REPRESSOR DNA-BINDING DOMAIN, NMR, 20 STRUCTURES'''
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===STRUCTURAL ROLE OF A BURIED SALT BRIDGE IN THE 434 REPRESSOR DNA-BINDING DOMAIN, NMR, 20 STRUCTURES===
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==Overview==
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The independently folding 63-residue N-terminal DNA-binding domain of the 434 repressor, 434(1-63), contains a buried Arg10-Glu35 salt bridge. A corresponding salt bridge is found in a variety of prokaryotic and eukaryotic DNA-binding proteins with helix-turn-helix motifs. Here, the NMR solution structures of 434(1-63) and the mutant protein 434[R10M](1-63) were determined to investigate the structural role of this salt bridge. Both proteins contain the same type of global fold, with five alpha-helices and a helix-turn-helix motif formed by the helices II and III. The primary structural difference caused by the Arg10 --&gt; Met mutation is a translation of helix I along its axis relative to the helix II-turn-helix III motif. This limited conformational change is paralleled by a 9 kJ M(-1) decrease of the stability of the folded mutant protein in aqueous solution at pH 4.8. It affects the pKa value of Glu19 as well as the population of a hydrogen bond between the backbone amide proton of Asn16 and the side-chain carboxylate group of Glu19. Using the crystal structure of the 434 repressor dimer complexed with the operator DNA as a basis, model building of the DNA complex with the NMR structure of 434[R10M](1-63) shows that Asn16, which is located on the protein surface, makes direct contact with the DNA and indicates that the point mutation Arg10 --&gt; Met should also lead to modifications of the protein-protein contacts in the complex.
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(as it appears on PubMed at http://www.pubmed.gov), where 9000626 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9000626}}
==About this Structure==
==About this Structure==
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1R63 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Phage_434 Phage 434]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R63 OCA].
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1R63 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Phage_434 Phage 434]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R63 OCA].
==Reference==
==Reference==
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[[Category: Helix-turn-helix]]
[[Category: Helix-turn-helix]]
[[Category: Phage 434 repressor]]
[[Category: Phage 434 repressor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:07:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:40:44 2008''

Revision as of 05:40, 29 July 2008

Image:1r63.png

Template:STRUCTURE 1r63

STRUCTURAL ROLE OF A BURIED SALT BRIDGE IN THE 434 REPRESSOR DNA-BINDING DOMAIN, NMR, 20 STRUCTURES

Template:ABSTRACT PUBMED 9000626

About this Structure

1R63 is a Single protein structure of sequence from Phage 434. Full experimental information is available from OCA.

Reference

Structural role of a buried salt bridge in the 434 repressor DNA-binding domain., Pervushin K, Billeter M, Siegal G, Wuthrich K, J Mol Biol. 1996 Dec 20;264(5):1002-12. PMID:9000626

Page seeded by OCA on Tue Jul 29 08:40:44 2008

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