1a7j
From Proteopedia
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Revision as of 12:41, 30 October 2007
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PHOSPHORIBULOKINASE FROM RHODOBACTER SPHEROIDES
Overview
The essential photosynthetic enzyme phosphoribulokinase (PRK) is, responsible for the conversion of ribulose 5-phosphate (Ru5P) to ribulose, 1,5-bisphosphate, the substrate for the CO2 fixing enzyme ribulose, 1,5-bisphosphate carboxylase/oxygenase (Rubisco). We have determined the, structure of the octameric bacterial form of PRK to a resolution of 2.5 A., The protein is folded into a seven-member mixed beta-sheet surrounded by, alpha-helices, giving the overall appearance of the nucleotide, monophosphate family of kinases. Homology with the nucleotide, monophosphate kinases suggests a number of amino acid residues that are, likely to be important in catalysis and suggests the roles of some amino, acid residues that have been mutated prior to the determination of the, structure. Further, ... [(full description)]
About this Structure
1A7J is a [Single protein] structure of sequence from [Rhodobacter sphaeroides] with SO4 as [ligand]. Active as [Phosphoribulokinase], with EC number [2.7.1.19]. Structure known Active Site: CIC. Full crystallographic information is available from [OCA].
Reference
The crystal structure of phosphoribulokinase from Rhodobacter sphaeroides reveals a fold similar to that of adenylate kinase., Harrison DH, Runquist JA, Holub A, Miziorko HM, Biochemistry. 1998 Apr 14;37(15):5074-85. PMID:9548738
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