1nbm: Difference between revisions

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-[[Image:1nbm.gif|left|200px]]<br />
-<applet load="1nbm" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1nbm, resolution 3.0&Aring;" />
-'''THE STRUCTURE OF BOVINE F1-ATPASE COVALENTLY INHIBITED WITH 4-CHLORO-7-NITROBENZOFURAZAN'''<br />
-==Overview==
+==THE STRUCTURE OF BOVINE F1-ATPASE COVALENTLY INHIBITED WITH 4-CHLORO-7-NITROBENZOFURAZAN==
-BACKGROUND: F1-ATPase is the globular domain of F1F0-ATP synthase that, catalyses the hydrolysis of ATP to ADP and phosphate. The crystal, structure of bovine F1-ATPase has been determined previously to 2.8 A, resolution. The enzyme comprises five different subunits in the, stoichiometry alpha 3 beta 3 gamma delta epsilon; the three catalytic beta, subunits alternate with the three alpha subunits around the centrally, located single gamma subunit. To understand more about the catalytic, mechanisms, F1-ATPase was inhibited by reaction with, 4-chloro-7-nitrobenzofurazan (NBD-Cl) and the structure of the inhibited, complex (F1-NBD) determined by X-ray crystallography. RESULTS: In the, structure the three beta subunits adopt a different conformation with, different nucleotide occupancy. ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9687365 (full description)]]
+<StructureSection load='1nbm' size='340' side='right'caption='[[1nbm]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1nbm]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NBM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NBM FirstGlance]. <br>
+</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&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TYN:AMINOBENZOFURAZAN-O-TYROSINE'>TYN</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nbm OCA], [https://pdbe.org/1nbm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nbm RCSB], [https://www.ebi.ac.uk/pdbsum/1nbm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nbm ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ATPA_BOVIN ATPA_BOVIN] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nb/1nbm_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1nbm ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-NBM is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]] with MG, PO4, ATP and ADP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.34 3.6.1.34]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NBM OCA]].
+*[[ATPase 3D structures|ATPase 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan: the structure provides further support for a rotary catalytic mechanism., Orriss GL, Leslie AG, Braig K, Walker JE, Structure. 1998 Jul 15;6(7):831-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9687365 9687365]
 [[Category: Bos taurus]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Braig, K.]]
+[[Category: Braig K]]
-[[Category: Leslie, A.G.W.]]
+[[Category: Leslie AGW]]
-[[Category: Orriss, G.L.]]
+[[Category: Orriss GL]]
-[[Category: Walker, J.E.]]
+[[Category: Walker JE]]
-[[Category: ADP]]
-[[Category: ATP]]
-[[Category: MG]]
-[[Category: PO4]]
-[[Category: 4-chloro-7-nitrobenzofurazan]]
-[[Category: atp synthase]]
-[[Category: f1-atpase]]
-[[Category: f1fo atp synthase]]
-[[Category: inhibition]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 16:15:17 2007''