1ibs: Difference between revisions
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|PDB= 1ibs |SIZE=350|CAPTION= <scene name='initialview01'>1ibs</scene>, resolution 2.8Å | |PDB= 1ibs |SIZE=350|CAPTION= <scene name='initialview01'>1ibs</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ABM:METHYL+PHOSPHONIC+ACID+ADENOSINE+ESTER'>ABM</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <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= PRS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | |GENE= PRS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1dkr|1DKR]], [[1dku|1DKU]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ibs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ibs OCA], [http://www.ebi.ac.uk/pdbsum/1ibs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ibs RCSB]</span> | |||
}} | }} | ||
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[[Category: Kadziola, A.]] | [[Category: Kadziola, A.]] | ||
[[Category: Larsen, S.]] | [[Category: Larsen, S.]] | ||
[[Category: domain duplication]] | [[Category: domain duplication]] | ||
[[Category: open alpha beta structure]] | [[Category: open alpha beta 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 21:17:31 2008'' | ||
Revision as of 21:17, 30 March 2008
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| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | PRS (Bacillus subtilis) | ||||||
| Activity: | Ribose-phosphate diphosphokinase, with EC number 2.7.6.1 | ||||||
| Related: | 1DKR, 1DKU
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PHOSPHORIBOSYLDIPHOSPHATE SYNTHETASE IN COMPLEX WITH CADMIUM IONS
OverviewOverview
The binding sites for the two cations essential for the catalytic function of 5-phospho-D-ribosyl alpha-1-diphosphate (PRPP) synthases have been identified from the structure of the Bacillus subtilis phosphoribosyldiphosphate synthetase (PRPPsase) with bound Cd(2+). The structure determined from X-ray diffraction data to 2.8-A resolution reveals the same hexameric arrangement of the subunits that was observed in the complexes of the enzyme with the activator sulfate and the allosteric inhibitor ADP. Two cation binding sites were localized in each of the two domains of the subunits that compose the hexamer; each domain of the subunit has an associated cation. In addition to the bound Cd(2+), the Cd(2+)-PRPPsase structure contains a sulfate ion in the regulatory site, a sulfate ion at the ribose-5-phosphate binding site, and an AMP moiety at the ATP binding site. Comparison of the Cd(2+)-PRPPsase to the structures of the PRPPsase complexed with sulfate and mADP reveals the structural rearrangement induced by the binding of the free cation, which is essential for the initiation of the reaction. The comparison to the cPRPP complex of glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli, a type I phosphoribosyltransferase, provided information about the binding of PRPP. This strongly indicates that the binding of both substrates must lead to a stabilized conformation of the loop region, which remains unresolved in the known PRPPsase complex structures.
About this StructureAbout this Structure
1IBS is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
ReferenceReference
Binding of cations in Bacillus subtilis phosphoribosyldiphosphate synthetase and their role in catalysis., Eriksen TA, Kadziola A, Larsen S, Protein Sci. 2002 Feb;11(2):271-9. PMID:11790837
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