1bmf: Difference between revisions
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[[Image:1bmf.gif|left|200px]]<br /> | [[Image:1bmf.gif|left|200px]]<br /><applet load="1bmf" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1bmf" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="1bmf, resolution 2.85Å" /> | caption="1bmf, resolution 2.85Å" /> | ||
'''BOVINE MITOCHONDRIAL F1-ATPASE'''<br /> | '''BOVINE MITOCHONDRIAL F1-ATPASE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1BMF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with MG, ANP and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_3.6.3.14 Transferred entry: 3.6.3.14], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.34 3.6.1.34] | 1BMF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with MG, ANP and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_3.6.3.14 Transferred entry: 3.6.3.14], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.34 3.6.1.34] Known structural/functional Sites: <scene name='pdbsite=CAT:The Carboxylate Group Of GLU Residue Is Believed To Acti ...'>CAT</scene> and <scene name='pdbsite=PLP:LYS Within The P-Loop (Phosphate Binding) Motif, Gxxxxgkt/S'>PLP</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BMF OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: f1fo atp synthase]] | [[Category: f1fo atp synthase]] | ||
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Revision as of 15:20, 18 December 2007
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BOVINE MITOCHONDRIAL F1-ATPASE
OverviewOverview
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 StructureAbout this Structure
1BMF is a Protein complex structure of sequences from Bos taurus with MG, ANP and ADP as ligands. Active as Transferred entry: 3.6.3.14, with EC number 3.6.1.34 Known structural/functional Sites: and . Full crystallographic information is available from OCA.
ReferenceReference
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:8065448
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