1bmf: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1bmf.gif|left|200px]]
-<!--
+==BOVINE MITOCHONDRIAL F1-ATPASE==
-The line below this paragraph, containing "STRUCTURE_1bmf", creates the "Structure Box" on the page.
+<StructureSection load='1bmf' size='340' side='right'caption='[[1bmf]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1bmf]] 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=1BMF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BMF FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85&#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=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-{{STRUCTURE_1bmf|  PDB=1bmf  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bmf OCA], [https://pdbe.org/1bmf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bmf RCSB], [https://www.ebi.ac.uk/pdbsum/1bmf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bmf 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/bm/1bmf_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=1bmf ConSurf].
+<div style="clear:both"></div>
-'''BOVINE MITOCHONDRIAL F1-ATPASE'''
+==See Also==
+*[[ATPase 3D structures|ATPase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-In the crystal structure of bovine mitochondrial F1-ATPase determined at 2.8 A resolution, the three catalytic beta-subunits differ in conformation and in the bound nucleotide. The structure supports a catalytic mechanism in intact ATP synthase in which the three catalytic subunits are in different states of the catalytic cycle at any instant. Interconversion of the states may be achieved by rotation of the alpha 3 beta 3 subassembly relative to an alpha-helical domain of the gamma-subunit.
-==About this Structure==
-BMF is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BMF OCA].
-==Reference==
-Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria., Abrahams JP, Leslie AG, Lutter R, Walker JE, Nature. 1994 Aug 25;370(6491):621-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8065448 8065448]
 [[Category: Bos taurus]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Abrahams, J P.]]
+[[Category: Abrahams JP]]
-[[Category: Leslie, A G.W.]]
+[[Category: Leslie AGW]]
-[[Category: Lutter, R.]]
+[[Category: Lutter R]]
-[[Category: Walker, J E.]]
+[[Category: Walker JE]]
-[[Category: Atp synthase]]
-[[Category: F1-atpase]]
-[[Category: F1fo atp synthase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:42:00 2008''