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2bq1

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Revision as of 13:15, 24 November 2021

Ribonucleotide reductase class 1b holocomplex R1E,R2F from Salmonella typhimurium

Structural highlights

2bq1 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1pem, 1peo, 1peq, 1peu, 1r2f, 2r2f
Activity:	Ribonucleoside-diphosphate reductase, with EC number 1.17.4.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RIR4_SALTY] Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R2F contains the tyrosyl radical required for catalysis.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Uppsten M, Farnegardh M, Domkin V, Uhlin U. The first holocomplex structure of ribonucleotide reductase gives new insight into its mechanism of action. J Mol Biol. 2006 Jun 2;359(2):365-77. Epub 2006 Mar 31. PMID:16631785 doi:10.1016/j.jmb.2006.03.035

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bq1"

@@ Line 3: / Line 3: @@
 <StructureSection load='2bq1' size='340' side='right'caption='[[2bq1]], [[Resolution|resolution]] 3.99&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2bq1]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BQ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BQ1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2bq1]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BQ1 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DGT:2-DEOXYGUANOSINE-5-TRIPHOSPHATE'>DGT</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DGT:2-DEOXYGUANOSINE-5-TRIPHOSPHATE'>DGT</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1pem|1pem]], [[1peo|1peo]], [[1peq|1peq]], [[1peu|1peu]], [[1r2f|1r2f]], [[2r2f|2r2f]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1pem|1pem]], [[1peo|1peo]], [[1peq|1peq]], [[1peu|1peu]], [[1r2f|1r2f]], [[2r2f|2r2f]]</div></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ribonucleoside-diphosphate_reductase Ribonucleoside-diphosphate reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.4.1 1.17.4.1] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bq1 OCA], [http://pdbe.org/2bq1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bq1 RCSB], [http://www.ebi.ac.uk/pdbsum/2bq1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bq1 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bq1 OCA], [https://pdbe.org/2bq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bq1 RCSB], [https://www.ebi.ac.uk/pdbsum/2bq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bq1 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RIR4_SALTY RIR4_SALTY]] Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R2F contains the tyrosyl radical required for catalysis.
+[[https://www.uniprot.org/uniprot/RIR4_SALTY RIR4_SALTY]] Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R2F contains the tyrosyl radical required for catalysis.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2bq1

From Proteopedia

Revision as of 13:15, 24 November 2021

Ribonucleotide reductase class 1b holocomplex R1E,R2F from Salmonella typhimurium

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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