1dkr
From Proteopedia
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|PDB= 1dkr |SIZE=350|CAPTION= <scene name='initialview01'>1dkr</scene>, resolution 2.30Å | |PDB= 1dkr |SIZE=350|CAPTION= <scene name='initialview01'>1dkr</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Ribose-phosphate_diphosphokinase Ribose-phosphate diphosphokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.6.1 2.7.6.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribose-phosphate_diphosphokinase Ribose-phosphate diphosphokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.6.1 2.7.6.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1dku|1DKU]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dkr OCA], [http://www.ebi.ac.uk/pdbsum/1dkr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dkr RCSB]</span> | ||
}} | }} | ||
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[[Category: Kadziola, A.]] | [[Category: Kadziola, A.]] | ||
[[Category: Larsen, S.]] | [[Category: Larsen, S.]] | ||
| - | [[Category: SO4]] | ||
[[Category: domain duplication]] | [[Category: domain duplication]] | ||
[[Category: open alpha beta domain structure]] | [[Category: open alpha beta domain structure]] | ||
[[Category: phosphoribosyltransferase type i fold.]] | [[Category: phosphoribosyltransferase type i fold.]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:43:28 2008'' |
Revision as of 16:43, 30 March 2008
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| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Ribose-phosphate diphosphokinase, with EC number 2.7.6.1 | ||||||
| Related: | 1DKU
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURES OF BACILLUS SUBTILIS PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE: MOLECULAR BASIS OF ALLOSTERIC INHIBITION AND ACTIVATION.
Overview
Here we report the first three-dimensional structure of a phosphoribosylpyrophosphate (PRPP) synthetase. PRPP is an essential intermediate in several biosynthetic pathways. Structures of the Bacillus subtilis PRPP synthetase in complex with analogs of the activator phosphate and the allosteric inhibitor ADP show that the functional form of the enzyme is a hexamer. The individual subunits fold into two domains, both of which resemble the type I phosphoribosyltransfereases. The active site is located between the two domains and includes residues from two subunits. Phosphate and ADP bind to the same regulatory site consisting of residues from three subunits of the hexamer. In addition to identifying residues important for binding substrates and effectors, the structures suggest a novel mode of allosteric regulation.
About this Structure
1DKR is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Structural basis for the function of Bacillus subtilis phosphoribosyl-pyrophosphate synthetase., Eriksen TA, Kadziola A, Bentsen AK, Harlow KW, Larsen S, Nat Struct Biol. 2000 Apr;7(4):303-8. PMID:10742175
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