1a7j

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[[Image:1a7j.gif|left|200px]]
[[Image:1a7j.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1a7j |SIZE=350|CAPTION= <scene name='initialview01'>1a7j</scene>, resolution 2.5&Aring;
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The line below this paragraph, containing "STRUCTURE_1a7j", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=CIC:Catalytic+Site'>CIC</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= PRKA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 Rhodobacter sphaeroides])
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-->
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|DOMAIN=
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{{STRUCTURE_1a7j| PDB=1a7j | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7j OCA], [http://www.ebi.ac.uk/pdbsum/1a7j PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a7j RCSB]</span>
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}}
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'''PHOSPHORIBULOKINASE FROM RHODOBACTER SPHEROIDES'''
'''PHOSPHORIBULOKINASE FROM RHODOBACTER SPHEROIDES'''
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[[Category: Miziorko, H.]]
[[Category: Miziorko, H.]]
[[Category: Runquist, J.]]
[[Category: Runquist, J.]]
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[[Category: calvin cycle]]
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[[Category: Calvin cycle]]
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[[Category: kinase]]
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[[Category: Kinase]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:55:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:34:56 2008''
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Revision as of 06:55, 2 May 2008

Template:STRUCTURE 1a7j

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 Page seeded by OCA on Fri May 2 09:55:51 2008

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