1xjj
From Proteopedia
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|PDB= 1xjj |SIZE=350|CAPTION= <scene name='initialview01'>1xjj</scene>, resolution 1.86Å | |PDB= 1xjj |SIZE=350|CAPTION= <scene name='initialview01'>1xjj</scene>, resolution 1.86Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= | + | |LIGAND= <scene name='pdbligand=DGT:2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE'>DGT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
- | |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] | + | |ACTIVITY= <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> |
|GENE= nrdj ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima]) | |GENE= nrdj ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1xje|1XJE]], [[1xjf|1XJF]], [[1xjg|1XJG]], [[1xjk|1XJK]], [[1xjm|1XJM]], [[1xjn|1XJN]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xjj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xjj OCA], [http://www.ebi.ac.uk/pdbsum/1xjj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xjj RCSB]</span> | ||
}} | }} | ||
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[[Category: Nordlund, P.]] | [[Category: Nordlund, P.]] | ||
[[Category: Reichard, P.]] | [[Category: Reichard, P.]] | ||
- | [[Category: DGT]] | ||
- | [[Category: MG]] | ||
[[Category: 10 alpha-beta barrel]] | [[Category: 10 alpha-beta barrel]] | ||
[[Category: allosteric regulation]] | [[Category: allosteric regulation]] | ||
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[[Category: substrate specificity]] | [[Category: substrate specificity]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:50:28 2008'' |
Revision as of 21:50, 30 March 2008
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, resolution 1.86Å | |||||||
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Ligands: | , | ||||||
Gene: | nrdj (Thermotoga maritima) | ||||||
Activity: | Ribonucleoside-diphosphate reductase, with EC number 1.17.4.1 | ||||||
Related: | 1XJE, 1XJF, 1XJG, 1XJK, 1XJM, 1XJN
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Structural mechanism of allosteric substrate specificity in a ribonucleotide reductase: dGTP complex
Overview
Ribonucleotide reductases (RNRs) catalyze the reduction of ribonucleotides into deoxyribonucleotides, which constitute the precursor pools used for DNA synthesis and repair. Imbalances in these pools increase mutational rates and are detrimental to the cell. Balanced precursor pools are maintained primarily through the regulation of the RNR substrate specificity. Here, the molecular mechanism of the allosteric substrate specificity regulation is revealed through the structures of a dimeric coenzyme B12-dependent RNR from Thermotoga maritima, both in complexes with four effector-substrate nucleotide pairs and in three complexes with only effector. The mechanism is based on the flexibility of loop 2, a key structural element, which forms a bridge between the specificity effector and substrate nucleotides. Substrate specificity is achieved as different effectors and their cognate substrates stabilize specific discrete loop 2 conformations. The mechanism of substrate specificity regulation is probably general for most class I and class II RNRs.
About this Structure
1XJJ is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
Structural mechanism of allosteric substrate specificity regulation in a ribonucleotide reductase., Larsson KM, Jordan A, Eliasson R, Reichard P, Logan DT, Nordlund P, Nat Struct Mol Biol. 2004 Nov;11(11):1142-9. Epub 2004 Oct 10. PMID:15475969
Page seeded by OCA on Mon Mar 31 00:50:28 2008
Categories: Ribonucleoside-diphosphate reductase | Single protein | Thermotoga maritima | Eliasson, R. | Jordan, A. | Larsson, K M. | Logan, D T. | Nordlund, P. | Reichard, P. | 10 alpha-beta barrel | Allosteric regulation | Protein-nucleotide complex | Ribonucleotide reductase | Substrate specificity