1mxr: Difference between revisions
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[[Image:1mxr.png|left|200px]] | [[Image:1mxr.png|left|200px]] | ||
{{STRUCTURE_1mxr| PDB=1mxr | SCENE= }} | {{STRUCTURE_1mxr| PDB=1mxr | SCENE= }} | ||
===High resolution structure of Ribonucleotide reductase R2 from E. coli in its oxidised (Met) form=== | ===High resolution structure of Ribonucleotide reductase R2 from E. coli in its oxidised (Met) form=== | ||
{{ABSTRACT_PUBMED_12624184}} | {{ABSTRACT_PUBMED_12624184}} | ||
==About this Structure== | ==About this Structure== | ||
[[1mxr]] is a 2 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=1MXR OCA]. | |||
==See Also== | |||
*[[Ribonucleotide reductase|Ribonucleotide reductase]] | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:012624184</ref><ref group="xtra">PMID:019061340</ref><references group="xtra"/> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Ribonucleoside-diphosphate reductase]] | [[Category: Ribonucleoside-diphosphate reductase]] | ||
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[[Category: Nordlund, P.]] | [[Category: Nordlund, P.]] | ||
[[Category: Di iron]] | [[Category: Di iron]] | ||
[[Category: Oxidoreductase]] | |||
[[Category: Radical protein]] | [[Category: Radical protein]] | ||
Revision as of 04:24, 27 July 2012
High resolution structure of Ribonucleotide reductase R2 from E. coli in its oxidised (Met) formHigh resolution structure of Ribonucleotide reductase R2 from E. coli in its oxidised (Met) form
Template:ABSTRACT PUBMED 12624184
About this StructureAbout this Structure
1mxr is a 2 chain structure of Ribonucleotide reductase with sequence from Escherichia coli. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
- ↑ Hogbom M, Galander M, Andersson M, Kolberg M, Hofbauer W, Lassmann G, Nordlund P, Lendzian F. Displacement of the tyrosyl radical cofactor in ribonucleotide reductase obtained by single-crystal high-field EPR and 1.4-A x-ray data. Proc Natl Acad Sci U S A. 2003 Mar 18;100(6):3209-14. Epub 2003 Mar 6. PMID:12624184 doi:10.1073/pnas.0536684100
- ↑ Jiang W, Yun D, Saleh L, Bollinger JM Jr, Krebs C. Formation and function of the Manganese(IV)/Iron(III) cofactor in Chlamydia trachomatis ribonucleotide reductase. Biochemistry. 2008 Dec 30;47(52):13736-44. PMID:19061340 doi:10.1021/bi8017625