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1qfn

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[[Image:1qfn.jpg|left|200px]]
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{{Seed}}
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[[Image:1qfn.png|left|200px]]
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{{STRUCTURE_1qfn| PDB=1qfn | SCENE= }}
{{STRUCTURE_1qfn| PDB=1qfn | SCENE= }}
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'''GLUTAREDOXIN-1-RIBONUCLEOTIDE REDUCTASE B1 MIXED DISULFIDE BOND'''
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===GLUTAREDOXIN-1-RIBONUCLEOTIDE REDUCTASE B1 MIXED DISULFIDE BOND===
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==Overview==
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The reduction equivalents necessary for the ribonucleotide reductase (RNR)-catalyzed production of deoxyribonucleotides are provided by glutaredoxin (Grx) or thioredoxin (Trx). The initial location for transfer of reducing equivalents to RNR is located at the C terminus of the B1 subunit and involves the reduction of a disulfide between Cys754 and Cys759. We have used a 25-mer peptide corresponding to residues 737-761 of RNR B1 (C754--&gt;S) to synthesize a stable mixed disulfide with Escherichia coli Grx-1 (C14--&gt;S) resembling the structure of an intermediate in the reaction. The high-resolution solution structure of the mixed disulfide has been obtained by NMR with an RMSD of 0.56 A for all the backbone atoms of the protein and the well-defined portion of the peptide. The binding interactions responsible for specificity have been identified demonstrating the importance of electrostatic interactions in this system and providing a rationale for the specificity of the Grx-RNR interaction. The disulfide is buried in this complex, implying a solely intra-molecular mechanism of reduction in contrast to the previously determined structure of the glutathione complex where the disulfide was exposed; mutagenesis studies have shown the relevance of intermolecular reduction processes. Substantial conformational changes in the helices of the protein are associated with peptide binding which have significant mechanistic implications for protein disulfide reduction by glutaredoxins.
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The line below this paragraph, {{ABSTRACT_PUBMED_10493864}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 10493864 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10493864}}
==About this Structure==
==About this Structure==
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1QFN is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QFN OCA].
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1QFN is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QFN OCA].
==Reference==
==Reference==
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[[Category: Glutaredoxin]]
[[Category: Glutaredoxin]]
[[Category: Ribonucleotide reductase]]
[[Category: Ribonucleotide reductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:12:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:30:59 2008''

Revision as of 21:31, 28 July 2008

Image:1qfn.png

Template:STRUCTURE 1qfn

GLUTAREDOXIN-1-RIBONUCLEOTIDE REDUCTASE B1 MIXED DISULFIDE BOND

Template:ABSTRACT PUBMED 10493864

About this Structure

1QFN is a Protein complex structure of sequences from Escherichia coli. Full experimental information is available from OCA.

Reference

Binding specificity and mechanistic insight into glutaredoxin-catalyzed protein disulfide reduction., Berardi MJ, Bushweller JH, J Mol Biol. 1999 Sep 10;292(1):151-61. PMID:10493864

Page seeded by OCA on Tue Jul 29 00:30:59 2008

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