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1l2p

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[[Image:1l2p.jpg|left|200px]]
 
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{{Structure
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==ATP Synthase b Subunit Dimerization Domain==
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|PDB= 1l2p |SIZE=350|CAPTION= <scene name='initialview01'>1l2p</scene>, resolution 1.55&Aring;
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<StructureSection load='1l2p' size='340' side='right'caption='[[1l2p]], [[Resolution|resolution]] 1.55&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'>[[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>
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|ACTIVITY= [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]
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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]] 1.55&#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=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>
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}}
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</table>
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== Function ==
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[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>
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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/l2/1l2p_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=1l2p ConSurf].
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<div style="clear:both"></div>
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'''ATP Synthase b Subunit Dimerization Domain'''
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==See Also==
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*[[ATPase 3D structures|ATPase 3D structures]]
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== References ==
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==Overview==
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<references/>
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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.
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__TOC__
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</StructureSection>
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==About this Structure==
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1L2P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The following page contains interesting information on the relation of 1L2P with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb72_1.html ATP Synthase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L2P OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12022893 12022893]
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[[Category: ATP Synthase]]
[[Category: ATP Synthase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Iron-chelate-transporting ATPase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Bi, Y.]]
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[[Category: Bi Y]]
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[[Category: Dunn, S D.]]
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[[Category: Del Rizzo PA]]
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[[Category: Rizzo, P A.Del.]]
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[[Category: Dunn SD]]
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[[Category: Shilton, B H.]]
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[[Category: Shilton BH]]
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[[Category: alpha helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:25:29 2008''
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Current revision

ATP Synthase b Subunit Dimerization Domain

PDB ID 1l2p

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