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| ==ESCHERICHIA COLI F1 ATPASE== | | ==ESCHERICHIA COLI F1 ATPASE== |
| <StructureSection load='1d8s' size='340' side='right' caption='[[1d8s]], [[Resolution|resolution]] 4.40Å' scene=''> | | <StructureSection load='1d8s' size='340' side='right'caption='[[1d8s]], [[Resolution|resolution]] 4.40Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[1d8s]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D8S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1D8S FirstGlance]. <br> | | <table><tr><td colspan='2'>[[1d8s]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D8S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D8S FirstGlance]. <br> |
| </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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]] 4.4Å</td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </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=1d8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d8s OCA], [https://pdbe.org/1d8s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d8s RCSB], [https://www.ebi.ac.uk/pdbsum/1d8s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d8s ProSAT]</span></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=1d8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d8s OCA], [http://pdbe.org/1d8s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1d8s RCSB], [http://www.ebi.ac.uk/pdbsum/1d8s PDBsum]</span></td></tr> | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The F(1) part of the F(1)F(O) ATP synthase from Escherichia coli has been crystallized and its structure determined to 4.4-A resolution by using molecular replacement based on the structure of the beef-heart mitochondrial enzyme. The bacterial F(1) consists of five subunits with stoichiometry alpha(3), beta(3), gamma, delta, and epsilon. delta was removed before crystallization. In agreement with the structure of the beef-heart mitochondrial enzyme, although not that from rat liver, the present study suggests that the alpha and beta subunits are arranged in a hexagonal barrel but depart from exact 3-fold symmetry. In the structures of both beef heart and rat-liver mitochondrial F(1), less than half of the structure of the gamma subunit was seen because of presumed disorder in the crystals. The present electron-density map includes a number of rod-shaped features which appear to correspond to additional alpha-helical regions within the gamma subunit. These suggest that the gamma subunit traverses the full length of the stalk that links the F(1) and F(O) parts and makes significant contacts with the c subunit ring of F(O).
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| Structural features of the gamma subunit of the Escherichia coli F(1) ATPase revealed by a 4.4-A resolution map obtained by x-ray crystallography.,Hausrath AC, Gruber G, Matthews BW, Capaldi RA Proc Natl Acad Sci U S A. 1999 Nov 23;96(24):13697-702. PMID:10570135<ref>PMID:10570135</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 1d8s" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[ATPase|ATPase]] | | *[[ATPase 3D structures|ATPase 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Bacillus coli migula 1895]] | | [[Category: Escherichia coli]] |
| [[Category: Capaldi, R A]] | | [[Category: Large Structures]] |
| [[Category: Gruber, G]] | | [[Category: Capaldi RA]] |
| [[Category: Hausrath, A C]] | | [[Category: Gruber G]] |
| [[Category: Matthews, B W]] | | [[Category: Hausrath AC]] |
| [[Category: Hydrolase]] | | [[Category: Matthews BW]] |