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| - | [[Image:1a7j.gif|left|200px]] | |
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| - | {{Structure
| + | ==PHOSPHORIBULOKINASE FROM RHODOBACTER SPHEROIDES== |
| - | |PDB= 1a7j |SIZE=350|CAPTION= <scene name='initialview01'>1a7j</scene>, resolution 2.5Å
| + | <StructureSection load='1a7j' size='340' side='right'caption='[[1a7j]], [[Resolution|resolution]] 2.50Å' scene=''> |
| - | |SITE= <scene name='pdbsite=CIC:Catalytic+Site'>CIC</scene>
| + | == Structural highlights == |
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
| + | <table><tr><td colspan='2'>[[1a7j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A7J FirstGlance]. <br> |
| - | |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>
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | |GENE= PRKA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 Rhodobacter sphaeroides])
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | |DOMAIN=
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7j OCA], [https://pdbe.org/1a7j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a7j RCSB], [https://www.ebi.ac.uk/pdbsum/1a7j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a7j ProSAT]</span></td></tr> |
| - | |RELATEDENTRY= | + | </table> |
| - | |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>
| + | == Function == |
| - | }}
| + | [https://www.uniprot.org/uniprot/KPPR1_CERSP KPPR1_CERSP] |
| - | | + | == Evolutionary Conservation == |
| - | '''PHOSPHORIBULOKINASE FROM RHODOBACTER SPHEROIDES'''
| + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | | + | Check<jmol> |
| - | | + | <jmolCheckbox> |
| - | ==Overview== | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a7/1a7j_consurf.spt"</scriptWhenChecked> |
| - | 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.
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | | + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | ==About this Structure== | + | </jmolCheckbox> |
| - | 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].
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a7j ConSurf]. |
| - | | + | <div style="clear:both"></div> |
| - | ==Reference==
| + | __TOC__ |
| - | 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]
| + | </StructureSection> |
| - | [[Category: Phosphoribulokinase]]
| + | [[Category: Cereibacter sphaeroides]] |
| - | [[Category: Rhodobacter sphaeroides]] | + | [[Category: Large Structures]] |
| - | [[Category: Single protein]] | + | [[Category: Harrison DHT]] |
| - | [[Category: Harrison, D H.T.]] | + | [[Category: Holub A]] |
| - | [[Category: Holub, A.]] | + | [[Category: Miziorko H]] |
| - | [[Category: Miziorko, H.]] | + | [[Category: Runquist J]] |
| - | [[Category: Runquist, J.]] | + | |
| - | [[Category: calvin cycle]]
| + | |
| - | [[Category: kinase]]
| + | |
| - | [[Category: transferase]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:34:56 2008''
| + | |
