3lg8
From Proteopedia
(Difference between revisions)
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- | + | ==Crystal structure of the C-terminal part of subunit E (E101-206) from Methanocaldococcus jannaschii of A1AO ATP synthase== | |
- | + | <StructureSection load='3lg8' size='340' side='right' caption='[[3lg8]], [[Resolution|resolution]] 4.10Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[3lg8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LG8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LG8 FirstGlance]. <br> | |
- | ==Function== | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2dm9|2dm9]], [[2dma|2dma]]</td></tr> |
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">atpE, MJ0220 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 ATCC 43067])</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=3lg8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lg8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lg8 RCSB], [http://www.ebi.ac.uk/pdbsum/3lg8 PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
[[http://www.uniprot.org/uniprot/VATE_METJA VATE_METJA]] Produces ATP from ADP in the presence of a proton gradient across the membrane (By similarity). | [[http://www.uniprot.org/uniprot/VATE_METJA VATE_METJA]] Produces ATP from ADP in the presence of a proton gradient across the membrane (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/lg/3lg8_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]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The structure of the C-terminus of subunit E (E(101-206)) of Methanocaldococcus jannaschii A-ATP synthase was determined at 4.1 A. E(101-206) consist of a N-terminal globular domain with three alpha-helices and four antiparallel beta-strands and an alpha-helix at the very C-terminus. Comparison of M. jannaschii E(101-206) with the C-terminus E(81-198) subunit E from Pyrococcus horikoshii OT3 revealed that the kink in the C-terminal alpha-helix of E(81-198), involved in dimer formation, is absent in M. jannaschii E(101-206). Whereas a major dimeric surface interface is present between the P. horikoshii E(81-198) molecules in the asymmetric unit, no such interaction could be found in the M. jannaschii E(101-206) molecules. To verify the oligomeric behaviour, the low resolution structure of the recombinant E(85-206) from M. jannaschii was determined using small angle X-ray scattering. Rigid body modeling of two copies of one of the monomer established a fit with a tail to tail arrangement. | ||
- | + | Crystal and solution structure of the C-terminal part of the Methanocaldococcus jannaschii A(1)A (O) ATP synthase subunit E revealed by X-ray diffraction and small-angle X-ray scattering.,Balakrishna AM, Manimekalai MS, Hunke C, Gayen S, Rossle M, Jeyakanthan J, Gruber G J Bioenerg Biomembr. 2010 Jun 23. PMID:20571891<ref>PMID:20571891</ref> | |
- | + | ||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
==See Also== | ==See Also== | ||
- | *[[ATP synthase|ATP synthase]] | ||
*[[ATPase|ATPase]] | *[[ATPase|ATPase]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | + | __TOC__ | |
+ | </StructureSection> | ||
[[Category: Atcc 43067]] | [[Category: Atcc 43067]] | ||
- | [[Category: Balakrishna, A M | + | [[Category: Balakrishna, A M]] |
- | [[Category: Gayen, S | + | [[Category: Gayen, S]] |
- | [[Category: Gruber, G | + | [[Category: Gruber, G]] |
- | [[Category: Hunke, C | + | [[Category: Hunke, C]] |
- | [[Category: Jeyakanthan, J | + | [[Category: Jeyakanthan, J]] |
- | [[Category: Manimekalai, M S.S | + | [[Category: Manimekalai, M S.S]] |
[[Category: Archaea]] | [[Category: Archaea]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] |
Revision as of 07:47, 24 December 2014
Crystal structure of the C-terminal part of subunit E (E101-206) from Methanocaldococcus jannaschii of A1AO ATP synthase
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