1l2p: Difference between revisions

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 ==ATP Synthase b Subunit Dimerization Domain==
-<StructureSection load='1l2p' size='340' side='right' caption='[[1l2p]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
+<StructureSection load='1l2p' size='340' side='right'caption='[[1l2p]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1l2p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. The December 2005 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''ATP Synthase''  by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2005_12 10.2210/rcsb_pdb/mom_2005_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L2P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L2P FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1l2p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The December 2005 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''ATP Synthase''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2005_12 10.2210/rcsb_pdb/mom_2005_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L2P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L2P FirstGlance]. <br>
-</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Iron-chelate-transporting_ATPase Iron-chelate-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.34 3.6.3.34] </span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l2p OCA], [http://pdbe.org/1l2p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1l2p RCSB], [http://www.ebi.ac.uk/pdbsum/1l2p PDBsum]</span></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=1l2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l2p OCA], [https://pdbe.org/1l2p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l2p RCSB], [https://www.ebi.ac.uk/pdbsum/1l2p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l2p ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ATPF_ECOLI ATPF_ECOLI]] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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 (By similarity).<ref>PMID:1682301</ref>   Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0) (By similarity).<ref>PMID:1682301</ref>
+[https://www.uniprot.org/uniprot/ATPF_ECOLI ATPF_ECOLI] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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 (By similarity).<ref>PMID:1682301</ref>   Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0) (By similarity).<ref>PMID:1682301</ref>
 == 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/l2/1l2p_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l2/1l2p_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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1l2p ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The b subunit of E. coli F(0)F(1)-ATPase links the peripheral F(1) subunits to the membrane-integral F(0) portion and functions as a "stator", preventing rotation of F(1). The b subunit is present as a dimer in ATP synthase, and residues 62-122 are required to mediate dimerization. To understand how the b subunit dimer is formed, we have studied the structure of the isolated dimerization domain, b(62-122). Analytical ultracentrifugation and solution small-angle X-ray scattering (SAXS) indicate that the b(62-122) dimer is extremely elongated, with a frictional ratio of 1.60, a maximal dimension of 95 A, and a radius of gyration of 27 A, values that are consistent with an alpha-helical coiled-coil structure. The crystal structure of b(62-122) has been solved and refined to 1.55 A. The protein crystallized as an isolated, monomeric alpha helix with a length of 90 A. Combining the crystal structure of monomeric b(62-122) with SAXS data from the dimer in solution, we have constructed a model for the b(62-122) dimer in which the two helices form a coiled coil with a right-handed superhelical twist. Analysis of b sequences from E. coli and other prokaryotes indicates conservation of an undecad repeat, which is characteristic of a right-handed coiled coil and consistent with our structural model. Mutation of residue Arg-83, which interrupts the undecad pattern, to alanine markedly stabilized the dimer, as expected for the proposed two-stranded, right-handed coiled-coil structure.
-The "second stalk" of Escherichia coli ATP synthase: structure of the isolated dimerization domain.,Del Rizzo PA, Bi Y, Dunn SD, Shilton BH Biochemistry. 2002 May 28;41(21):6875-84. PMID:12022893<ref>PMID:12022893</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1l2p" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[ATPase|ATPase]]
+*[[ATPase 3D structures|ATPase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
 [[Category: ATP Synthase]]
-[[Category: Iron-chelate-transporting ATPase]]
+[[Category: Escherichia coli]]
+[[Category: Large Structures]]
 [[Category: RCSB PDB Molecule of the Month]]
-[[Category: Bi, Y]]
+[[Category: Bi Y]]
-[[Category: Dunn, S D]]
+[[Category: Del Rizzo PA]]
-[[Category: Rizzo, P A.Del]]
+[[Category: Dunn SD]]
-[[Category: Shilton, B H]]
+[[Category: Shilton BH]]
-[[Category: Alpha helix]]
-[[Category: Hydrolase]]