1kgp: Difference between revisions
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'''R2F from Corynebacterium Ammoniagenes in its Mn substituted form''' | {{Structure | ||
|PDB= 1kgp |SIZE=350|CAPTION= <scene name='initialview01'>1kgp</scene>, resolution 2.00Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''R2F from Corynebacterium Ammoniagenes in its Mn substituted form''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1KGP is a [ | 1KGP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Corynebacterium_ammoniagenes Corynebacterium ammoniagenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KGP OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11802741 11802741] | ||
[[Category: Corynebacterium ammoniagenes]] | [[Category: Corynebacterium ammoniagenes]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: radical protein]] | [[Category: radical protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:17:14 2008'' | ||
Revision as of 13:17, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
R2F from Corynebacterium Ammoniagenes in its Mn substituted form
OverviewOverview
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.
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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