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1fx0

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[[Image:1fx0.gif|left|200px]]
 
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{{Structure
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==Crystal structure of the chloroplast F1-ATPase from spinach==
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|PDB= 1fx0 |SIZE=350|CAPTION= <scene name='initialview01'>1fx0</scene>, resolution 3.2&Aring;
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<StructureSection load='1fx0' size='340' side='right'caption='[[1fx0]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1fx0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FX0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FX0 FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
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|GENE=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fx0 OCA], [https://pdbe.org/1fx0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fx0 RCSB], [https://www.ebi.ac.uk/pdbsum/1fx0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fx0 ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fx0 OCA], [http://www.ebi.ac.uk/pdbsum/1fx0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fx0 RCSB]</span>
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[https://www.uniprot.org/uniprot/ATPA_SPIOL ATPA_SPIOL] Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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'''Crystal structure of the chloroplast F1-ATPase from spinach'''
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fx/1fx0_consurf.spt"</scriptWhenChecked>
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==Overview==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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The structure of the F(1)-ATPase from spinach chloroplasts was determined to 3.2 A resolution by molecular replacement based on the homologous structure of the bovine mitochondrial enzyme. The crystallized complex contains four different subunits in a stoichiometry of alpha(3)beta(3)gammaepsilon. Subunit delta was removed before crystallization to improve the diffraction of the crystals. The overall structure of the noncatalytic alpha-subunits and the catalytic beta-subunits is highly similar to those of the mitochondrial and thermophilic subunits. However, in the crystal structure of the chloroplast enzyme, all alpha- and beta-subunits adopt a closed conformation and appear to contain no bound adenine nucleotides. The superimposed crystallographic symmetry in the space group R32 impaired an exact tracing of the gamma- and epsilon-subunits in the complex. However, clear electron density was present at the core of the alpha(3)beta(3)-subcomplex, which probably represents the C-terminal domain of the gamma-subunit. The structure of the spinach chloroplast F(1) has a potential binding site for the phytotoxin, tentoxin, at the alphabeta-interface near betaAsp(83) and an insertion from betaGly(56)-Asn(60) in the N-terminal beta-barrel domain probably increases the thermal stability of the complex. The structure probably represents an inactive latent state of the ATPase, which is unique to chloroplast and cyanobacterial enzymes.
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==About this Structure==
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</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=1fx0 ConSurf].
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1FX0 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FX0 OCA].
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<div style="clear:both"></div>
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__TOC__
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==Reference==
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</StructureSection>
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The structure of the chloroplast F1-ATPase at 3.2 A resolution., Groth G, Pohl E, J Biol Chem. 2001 Jan 12;276(2):1345-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11032839 11032839]
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[[Category: Large Structures]]
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[[Category: H(+)-transporting two-sector ATPase]]
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[[Category: Protein complex]]
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[[Category: Spinacia oleracea]]
[[Category: Spinacia oleracea]]
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[[Category: Groth, G.]]
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[[Category: Groth G]]
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[[Category: Pohl, E.]]
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[[Category: Pohl E]]
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[[Category: latent atpase]]
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[[Category: potential tentoxin binding site]]
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[[Category: thermal stability]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:31:56 2008''
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Current revision

Crystal structure of the chloroplast F1-ATPase from spinach

PDB ID 1fx0

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