1biq

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[[Image:1biq.gif|left|200px]]<br /><applet load="1biq" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1biq.gif|left|200px]]
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caption="1biq, resolution 2.05&Aring;" />
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'''RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 1 BETA CHAIN MUTANT E238A'''<br />
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{{Structure
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|PDB= 1biq |SIZE=350|CAPTION= <scene name='initialview01'>1biq</scene>, resolution 2.05&Aring;
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|SITE= <scene name='pdbsite=FE1:Diiron+Cluster+In+Chain+A'>FE1</scene> and <scene name='pdbsite=FE2:Diiron+Cluster+In+Chain+B'>FE2</scene>
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|LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene> and <scene name='pdbligand=HG:MERCURY (II) ION'>HG</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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'''RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 1 BETA CHAIN MUTANT E238A'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1BIQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=FE2:'>FE2</scene>, <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=OH:'>OH</scene> and <scene name='pdbligand=HG:'>HG</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 Sites: <scene name='pdbsite=FE1:Diiron+Cluster+In+Chain+A'>FE1</scene> and <scene name='pdbsite=FE2:Diiron+Cluster+In+Chain+B'>FE2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BIQ OCA].
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1BIQ is a [[Protein complex]] structure of sequences 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=1BIQ OCA].
==Reference==
==Reference==
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Crystal structures of two self-hydroxylating ribonucleotide reductase protein R2 mutants: structural basis for the oxygen-insertion step of hydroxylation reactions catalyzed by diiron proteins., Logan DT, deMare F, Persson BO, Slaby A, Sjoberg BM, Nordlund P, Biochemistry. 1998 Jul 28;37(30):10798-807. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9692970 9692970]
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Crystal structures of two self-hydroxylating ribonucleotide reductase protein R2 mutants: structural basis for the oxygen-insertion step of hydroxylation reactions catalyzed by diiron proteins., Logan DT, deMare F, Persson BO, Slaby A, Sjoberg BM, Nordlund P, Biochemistry. 1998 Jul 28;37(30):10798-807. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9692970 9692970]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:55:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:11:31 2008''

Revision as of 08:11, 20 March 2008

Image:1biq.gif


PDB ID 1biq

Drag the structure with the mouse to rotate
, resolution 2.05Å
Sites: and
Ligands: , , and
Activity: Ribonucleoside-diphosphate reductase, with EC number 1.17.4.1
Coordinates: save as pdb, mmCIF, xml



RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 1 BETA CHAIN MUTANT E238A


Overview

The R2 protein of ribonucleotide reductase catalyzes the dioxygen-dependent one-electron oxidation of Tyr122 at a diiron-carboxylate site. Methane monooxygenase and related hydroxylases catalyze hydrocarbon hydroxylation at diiron sites structurally related to the one in R2. In protein R2, the likely reaction site for dioxygen is close to Phe208. The crystal structure of an iron ligand mutant R2, Y122F/E238A, reveals the hydroxylation of Phe208 at the meta, or epsilon-, ring position and the subsequent coordination of this residue to the diiron site. In another mutant, F208Y, the "foreign" residue Tyr208 is hydroxylated to Dopa. The structures of apo and diferrous F208Y presented here suggest that Tyr208 is coordinated to the iron site of F208Y throughout the Dopa generation cycle. Together, the structural data on these two mutants suggest two possible reaction geometries for the hydroxylation reaction catalyzed by these modified R2 diiron sites, geometries which might be relevant for the hydroxylation reaction catalyzed by other diiron sites such as methane monooxygenase. A critical role for residue Glu238 in directing the oxidative power of the reactive intermediate toward oxidation of Tyr122 is proposed.

About this Structure

1BIQ is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structures of two self-hydroxylating ribonucleotide reductase protein R2 mutants: structural basis for the oxygen-insertion step of hydroxylation reactions catalyzed by diiron proteins., Logan DT, deMare F, Persson BO, Slaby A, Sjoberg BM, Nordlund P, Biochemistry. 1998 Jul 28;37(30):10798-807. PMID:9692970

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