1a7j
From Proteopedia
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- | [[Image:1a7j.gif|left|200px]] | + | [[Image:1a7j.gif|left|200px]] |
- | + | ||
- | '''PHOSPHORIBULOKINASE FROM RHODOBACTER SPHEROIDES''' | + | {{Structure |
+ | |PDB= 1a7j |SIZE=350|CAPTION= <scene name='initialview01'>1a7j</scene>, resolution 2.5Å | ||
+ | |SITE= <scene name='pdbsite=CIC:Catalytic+Site'>CIC</scene> | ||
+ | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
+ | |ACTIVITY= [http://en.wikipedia.org/wiki/Phosphoribulokinase Phosphoribulokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.19 2.7.1.19] | ||
+ | |GENE= PRKA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 Rhodobacter sphaeroides]) | ||
+ | }} | ||
+ | |||
+ | '''PHOSPHORIBULOKINASE FROM RHODOBACTER SPHEROIDES''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1A7J is a [ | + | 1A7J is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7J OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9548738 9548738] |
[[Category: Phosphoribulokinase]] | [[Category: Phosphoribulokinase]] | ||
[[Category: Rhodobacter sphaeroides]] | [[Category: Rhodobacter sphaeroides]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:54:03 2008'' |
Revision as of 07:54, 20 March 2008
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, resolution 2.5Å | |||||||
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Sites: | |||||||
Ligands: | |||||||
Gene: | PRKA (Rhodobacter sphaeroides) | ||||||
Activity: | Phosphoribulokinase, with EC number 2.7.1.19 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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, sequence identity across eukaryotic and prokaryotic species and a calculation of the buried surface area suggests the identity within the octamer of a dimer conserved throughout evolution. The width of the groove leading to the active site is consistent with an oriented molecule of thioredoxin controlling the oxidation state of two cysteines that regulate activity in the eukaryotic enzymes. Although neither Asp 42 nor Asp 169 can be definitively assigned as the catalytic base, the crystal structure suggests the location of a ribulose 5-phosphate binding site and suggests a role for several of the conserved basic residues.
About this Structure
1A7J is a Single protein structure of sequence from Rhodobacter sphaeroides. 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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