1kgp: Difference between revisions

Revision as of 10:19, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1kgp.png

Template:STRUCTURE 1kgp

R2F from Corynebacterium Ammoniagenes in its Mn substituted formR2F from Corynebacterium Ammoniagenes in its Mn substituted form

Template:ABSTRACT PUBMED 11802741

About this StructureAbout this Structure

1KGP is a Single protein structure of sequence from Corynebacterium ammoniagenes. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the di-iron/radical protein of ribonucleotide reductase from Corynebacterium ammoniagenes., Hogbom M, Huque Y, Sjoberg BM, Nordlund P, Biochemistry. 2002 Jan 29;41(4):1381-9. PMID:11802741

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''R2F from Corynebacterium Ammoniagenes in its Mn substituted form'''
+===R2F from Corynebacterium Ammoniagenes in its Mn substituted form===
-==Overview==
+<!--
-Ribonucleotide reductase (RNR) is the enzyme performing de novo production of the four deoxyribonucleotides needed for DNA synthesis. All mammals as well as some prokaryotes express the class I enzyme which is an alpha(2)beta(2) protein. The smaller of the homodimers, denoted R2, contains a di-iron carboxylate site which, upon reaction with molecular oxygen, generates a stable tyrosyl radical needed for catalysis. The three-dimensional structure of the oxidized class Ib RNR R2 from Corynebacterium ammoniagenes has been determined at 1.85 A resolution and refined to an R-value of 15.8% (R(free) = 21.3%). In addition, structures of both the reduced iron-containing, and manganese-substituted protein have been solved. The C. ammoniagenes R2 has been proposed to be manganese-dependent. The present structure provides evidence that manganese is not oxidized by the protein, in agreement with recent biochemical data, and that no obvious structural abnormalities are seen in the oxidized and reduced iron-containing forms, giving further support that the protein is indeed an iron-dependent RNR R2. The di-manganese structure also provides an explanation for the magnetic properties of this site. The structure of the oxidized C. ammoniagenes R2 also reveals an additional water molecule bridging the radical and the iron site, which has not previously been seen in any other R2 structure and which might have important mechanistic implications.
+The line below this paragraph, {{ABSTRACT_PUBMED_11802741}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11802741 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11802741}}
 ==About this Structure==
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 [[Category: Helix bundle]]
 [[Category: Radical protein]]
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