2xo5
From Proteopedia
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[[Image:2xo5.png|left|200px]] | [[Image:2xo5.png|left|200px]] | ||
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{{STRUCTURE_2xo5| PDB=2xo5 | SCENE= }} | {{STRUCTURE_2xo5| PDB=2xo5 | SCENE= }} | ||
===RIBONUCLEOTIDE REDUCTASE Y731NH2Y MODIFIED R1 SUBUNIT OF E. COLI=== | ===RIBONUCLEOTIDE REDUCTASE Y731NH2Y MODIFIED R1 SUBUNIT OF E. COLI=== | ||
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{{ABSTRACT_PUBMED_21612216}} | {{ABSTRACT_PUBMED_21612216}} | ||
==About this Structure== | ==About this Structure== | ||
| - | [[2xo5]] is a 7 chain structure with sequence 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=2XO5 OCA]. | + | [[2xo5]] is a 7 chain structure of [[Ribonucleotide reductase]] with sequence 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=2XO5 OCA]. |
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| + | ==See Also== | ||
| + | *[[Ribonucleotide reductase|Ribonucleotide reductase]] | ||
==Reference== | ==Reference== | ||
Revision as of 15:51, 25 July 2012
Contents |
RIBONUCLEOTIDE REDUCTASE Y731NH2Y MODIFIED R1 SUBUNIT OF E. COLI
Template:ABSTRACT PUBMED 21612216
About this Structure
2xo5 is a 7 chain structure of Ribonucleotide reductase with sequence from Escherichia coli. Full crystallographic information is available from OCA.
See Also
Reference
- Minnihan EC, Seyedsayamdost MR, Uhlin U, Stubbe J. Kinetics of Radical Intermediate Formation and Deoxynucleotide Production in 3-Aminotyrosine-Substituted Escherichia coli Ribonucleotide Reductases. J Am Chem Soc. 2011 Jun 22;133(24):9430-40. Epub 2011 May 25. PMID:21612216 doi:10.1021/ja201640n
- Uhlin U, Eklund H. Structure of ribonucleotide reductase protein R1. Nature. 1994 Aug 18;370(6490):533-9. PMID:8052308 doi:http://dx.doi.org/10.1038/370533a0
- Eriksson M, Uhlin U, Ramaswamy S, Ekberg M, Regnstrom K, Sjoberg BM, Eklund H. Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding. Structure. 1997 Aug 15;5(8):1077-92. PMID:9309223
