1l2p: Difference between revisions
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'''ATP Synthase b Subunit Dimerization Domain''' | {{Structure | ||
|PDB= 1l2p |SIZE=350|CAPTION= <scene name='initialview01'>1l2p</scene>, resolution 1.55Å | |||
|SITE= | |||
|LIGAND= | |||
|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] | |||
|GENE= | |||
}} | |||
'''ATP Synthase b Subunit Dimerization Domain''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1L2P is a [ | 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]. | ||
==Reference== | ==Reference== | ||
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:// | 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] | ||
[[Category: ATP Synthase]] | [[Category: ATP Synthase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: alpha helix]] | [[Category: alpha helix]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:25:29 2008'' | ||
Revision as of 13:25, 20 March 2008
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| , resolution 1.55Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Iron-chelate-transporting ATPase, with EC number 3.6.3.34 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ATP Synthase b Subunit Dimerization Domain
OverviewOverview
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.
About this StructureAbout this Structure
1L2P is a Single protein structure of sequence from Escherichia coli. The following page contains interesting information on the relation of 1L2P with [ATP Synthase]. Full crystallographic information is available from OCA.
ReferenceReference
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:12022893
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