2bq1

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[[Image:2bq1.gif|left|200px]]<br /><applet load="2bq1" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2bq1.gif|left|200px]]
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caption="2bq1, resolution 3.99&Aring;" />
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'''RIBONUCLEOTIDE REDUCTASE CLASS 1B HOLOCOMPLEX R1E,R2F FROM SALMONELLA TYPHIMURIUM'''<br />
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{{Structure
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|PDB= 2bq1 |SIZE=350|CAPTION= <scene name='initialview01'>2bq1</scene>, resolution 3.99&Aring;
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|SITE= <scene name='pdbsite=AC1:Fe+Binding+Site+For+Chain+J'>AC1</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> and <scene name='pdbligand=DGT:2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE'>DGT</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Ribonucleoside-diphosphate_reductase Ribonucleoside-diphosphate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.4.1 1.17.4.1]
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|GENE=
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}}
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'''RIBONUCLEOTIDE REDUCTASE CLASS 1B HOLOCOMPLEX R1E,R2F FROM SALMONELLA TYPHIMURIUM'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2BQ1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=FE:'>FE</scene> and <scene name='pdbligand=DGT:'>DGT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ribonucleoside-diphosphate_reductase Ribonucleoside-diphosphate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.4.1 1.17.4.1] Known structural/functional Site: <scene name='pdbsite=AC1:Fe+Binding+Site+For+Chain+J'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BQ1 OCA].
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2BQ1 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BQ1 OCA].
==Reference==
==Reference==
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The first holocomplex structure of ribonucleotide reductase gives new insight into its mechanism of action., Uppsten M, Farnegardh M, Domkin V, Uhlin U, J Mol Biol. 2006 Jun 2;359(2):365-77. Epub 2006 Mar 31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16631785 16631785]
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The first holocomplex structure of ribonucleotide reductase gives new insight into its mechanism of action., Uppsten M, Farnegardh M, Domkin V, Uhlin U, J Mol Biol. 2006 Jun 2;359(2):365-77. Epub 2006 Mar 31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16631785 16631785]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Ribonucleoside-diphosphate reductase]]
[[Category: Ribonucleoside-diphosphate reductase]]
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[[Category: ribonucleotide reductase]]
[[Category: ribonucleotide reductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:40:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:05:10 2008''

Revision as of 14:05, 20 March 2008

Image:2bq1.gif


PDB ID 2bq1

Drag the structure with the mouse to rotate
, resolution 3.99Å
Sites:
Ligands: , and
Activity: Ribonucleoside-diphosphate reductase, with EC number 1.17.4.1
Coordinates: save as pdb, mmCIF, xml



RIBONUCLEOTIDE REDUCTASE CLASS 1B HOLOCOMPLEX R1E,R2F FROM SALMONELLA TYPHIMURIUM


Overview

Ribonucleotide reductase is an indispensable enzyme for all cells, since it catalyses the biosynthesis of the precursors necessary for both building and repairing DNA. The ribonucleotide reductase class I enzymes, present in all mammals as well as in many prokaryotes and DNA viruses, are composed mostly of two homodimeric proteins, R1 and R2. The reaction involves long-range radical transfer between the two proteins. Here, we present the first crystal structure of a ribonucleotide reductase R1/R2 holocomplex. The biological relevance of this complex is based on the binding of the R2 C terminus in the hydrophobic cleft of R1, an interaction proven to be crucial for enzyme activity, and by the fact that all conserved amino acid residues in R2 are facing the R1 active sites. We suggest that the asymmetric R1/R2 complex observed in the 4A crystal structure of Salmonella typhimurium ribonucleotide reductase represents an intermediate stage in the reaction cycle, and at the moment of reaction the homodimers transiently form a tight symmetric complex.

About this Structure

2BQ1 is a Protein complex structure of sequences from Salmonella typhimurium. Full crystallographic information is available from OCA.

Reference

The first holocomplex structure of ribonucleotide reductase gives new insight into its mechanism of action., Uppsten M, Farnegardh M, Domkin V, Uhlin U, J Mol Biol. 2006 Jun 2;359(2):365-77. Epub 2006 Mar 31. PMID:16631785

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