1uzr

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{{STRUCTURE_1uzr| PDB=1uzr | SCENE= }}
{{STRUCTURE_1uzr| PDB=1uzr | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE CLASS IB RIBONUCLEOTIDE REDUCTASE R2F-2 SUBUNIT FROM MYCOBACTERIUM TUBERCULOSIS'''
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===CRYSTAL STRUCTURE OF THE CLASS IB RIBONUCLEOTIDE REDUCTASE R2F-2 SUBUNIT FROM MYCOBACTERIUM TUBERCULOSIS===
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==Overview==
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Two nrdF genes of Mycobacterium tuberculosis code for different R2 subunits of the class Ib ribonucleotide reductase (RNR). The proteins are denoted R2F-1 and R2F-2 having 71% sequence identity. The R2F-2 subunit forms the biologically active RNR complex with the catalytic R1E-subunit. We present the structure of the reduced R2F-2 subunit to 2.2 A resolution. Comparison of the R2F-2 structure with a model of R2F-1 suggests that the important differences are located at the C-terminus. We found that within class Ib, the E-helix close to the iron diiron centre has two preferred conformations, which cannot be explained by the redox-state of the diiron centre. In the R2F-2 structure, we also could see a mobility of alphaE in between the two conformations.
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(as it appears on PubMed at http://www.pubmed.gov), where 15225619 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15225619}}
==About this Structure==
==About this Structure==
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[[Category: Small subunit]]
[[Category: Small subunit]]
[[Category: Tuberculosis]]
[[Category: Tuberculosis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:54:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:48:34 2008''

Revision as of 12:48, 28 July 2008

Image:1uzr.png

Template:STRUCTURE 1uzr

CRYSTAL STRUCTURE OF THE CLASS IB RIBONUCLEOTIDE REDUCTASE R2F-2 SUBUNIT FROM MYCOBACTERIUM TUBERCULOSIS

Template:ABSTRACT PUBMED 15225619

About this Structure

1UZR is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Crystal structure of the biologically active form of class Ib ribonucleotide reductase small subunit from Mycobacterium tuberculosis., Uppsten M, Davis J, Rubin H, Uhlin U, FEBS Lett. 2004 Jul 2;569(1-3):117-22. PMID:15225619

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