1l2p

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[[Image:1l2p.jpg|left|200px]]
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[[Image:1l2p.png|left|200px]]
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==Overview==
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{{ABSTRACT_12022893}}
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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.
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==About this Structure==
==About this Structure==
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].
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].
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==Reference==
 
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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: Shilton, B H.]]
[[Category: Shilton, B H.]]
[[Category: Alpha helix]]
[[Category: Alpha helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:28:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 17:39:51 2008''

Revision as of 14:39, 26 June 2008

Image:1l2p.png

Template:STRUCTURE 1l2p

ATP Synthase b Subunit Dimerization Domain


Template:ABSTRACT 12022893

About 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.

Page seeded by OCA on Thu Jun 26 17:39:51 2008

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