1fs0

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(New page: 200px<br /><applet load="1fs0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fs0, resolution 2.1&Aring;" /> '''COMPLEX OF GAMMA/EPSI...)
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[[Image:1fs0.jpg|left|200px]]<br /><applet load="1fs0" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fs0, resolution 2.1&Aring;" />
 
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'''COMPLEX OF GAMMA/EPSILON ATP SYNTHASE FROM E.COLI'''<br />
 
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==Overview==
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==COMPLEX OF GAMMA/EPSILON ATP SYNTHASE FROM E.COLI==
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ATP synthases (F(1)F(o)-ATPases) use energy released by the movement of, protons down a transmembrane electrochemical gradient to drive the, synthesis of ATP, the universal biological energy currency. Proton flow, through F(o) drives rotation of a ring of c-subunits and a complex of the, gamma and epsilon-subunits, causing cyclical conformational changes in, F(1) that are required for catalysis. The crystal structure of a large, portion of F(1) has been resolved. However, the structure of the central, portion of the enzyme, through which conformational changes in F(o) are, communicated to F(1), has until now remained elusive. Here we report the, crystal structure of a complex of the epsilon-subunit and the central, domain of the gamma-subunit refined at 2.1 A resolution. The structure, reveals how rotation of these subunits causes large conformational changes, in F(1), and thereby provides new insights into energy coupling between, F(o) and F(1).
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<StructureSection load='1fs0' size='340' side='right'caption='[[1fs0]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1fs0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FS0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FS0 FirstGlance]. <br>
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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]] 2.1&#8491;</td></tr>
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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=1fs0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fs0 OCA], [https://pdbe.org/1fs0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fs0 RCSB], [https://www.ebi.ac.uk/pdbsum/1fs0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fs0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ATPE_ECOLI ATPE_ECOLI] Produces ATP from ADP in the presence of a proton gradient across the membrane.[HAMAP-Rule:MF_00530]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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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/fs/1fs0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1fs0 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1FS0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FS0 OCA].
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*[[ATPase 3D structures|ATPase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structure of the gamma-epsilon complex of ATP synthase., Rodgers AJ, Wilce MC, Nat Struct Biol. 2000 Nov;7(11):1051-4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11062562 11062562]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: H(+)-transporting two-sector ATPase]]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Rodgers AJW]]
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[[Category: Rodgers, A.J.W.]]
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[[Category: Wilce MCJ]]
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[[Category: Wilce, M.C.J.]]
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[[Category: atp synthase]]
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[[Category: coiled coil]]
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[[Category: epsilon]]
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[[Category: gamma]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:13:09 2007''
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Current revision

COMPLEX OF GAMMA/EPSILON ATP SYNTHASE FROM E.COLI

PDB ID 1fs0

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