2cly
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [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] | + | |ACTIVITY= <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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cly OCA], [http://www.ebi.ac.uk/pdbsum/2cly PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cly RCSB]</span> | ||
}} | }} | ||
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[[Category: atp synthase]] | [[Category: atp synthase]] | ||
[[Category: cf(0)]] | [[Category: cf(0)]] | ||
| - | [[Category: hydrogen ion transport]] | + | [[Category: hydrogen ion transport,transit peptide]] |
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: ion transport]] | [[Category: ion transport]] | ||
| Line 38: | Line 41: | ||
[[Category: peripheral stalk]] | [[Category: peripheral stalk]] | ||
[[Category: stator]] | [[Category: stator]] | ||
| - | [[Category: transit peptide]] | ||
[[Category: transport]] | [[Category: transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:23:23 2008'' |
Revision as of 23:23, 30 March 2008
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| , resolution 2.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SUBCOMPLEX OF THE STATOR OF BOVINE MITOCHONDRIAL ATP SYNTHASE
Overview
The structure of most of the peripheral stalk, or stator, of the F-ATPase from bovine mitochondria, determined at 2.8 A resolution, contains residues 79-183, 3-123 and 5-70 of subunits b, d and F6, respectively. It consists of a continuous curved alpha-helix about 160 A long in the single b-subunit, augmented by the predominantly alpha-helical d- and F6-subunits. The structure occupies most of the peripheral stalk in a low-resolution structure of the F-ATPase. The long helix in subunit b extends from near to the top of the F1 domain to the surface of the membrane domain, and it probably continues unbroken across the membrane. Its uppermost region interacts with the oligomycin sensitivity conferral protein, bound to the N-terminal region of one alpha-subunit in the F1 domain. Various features suggest that the peripheral stalk is probably rigid rather than resembling a flexible rope. It remains unclear whether the transient storage of energy required by the rotary mechanism takes place in the central stalk or in the peripheral stalk or in both domains.
About this Structure
2CLY is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.
Reference
On the structure of the stator of the mitochondrial ATP synthase., Dickson VK, Silvester JA, Fearnley IM, Leslie AG, Walker JE, EMBO J. 2006 Jun 21;25(12):2911-8. Epub 2006 Jun 8. PMID:16791136
Page seeded by OCA on Mon Mar 31 02:23:23 2008
Categories: Bos taurus | H(+)-transporting two-sector ATPase | Protein complex | Dickson, V Kane. | Fearnley, I M. | Leslie, A G.W. | Silvester, J A. | Walker, J E. | Acetylation | Atp synthase | Cf(0) | Hydrogen ion transport,transit peptide | Hydrolase | Ion transport | Mitochondria | Mitochondrion | Peripheral stalk | Stator | Transport
