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1l2p
From Proteopedia
(New page: 200px<br /> <applet load="1l2p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l2p, resolution 1.55Å" /> '''ATP Synthase b Subu...) |
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caption="1l2p, resolution 1.55Å" /> | caption="1l2p, resolution 1.55Å" /> | ||
'''ATP Synthase b Subunit Dimerization Domain'''<br /> | '''ATP Synthase b Subunit Dimerization Domain'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1L2P is a [http://en.wikipedia.org/wiki/Single_protein 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]]. Active as [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] Full crystallographic information is available from [http:// | + | 1L2P is a [http://en.wikipedia.org/wiki/Single_protein 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]]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L2P OCA]. |
==Reference== | ==Reference== | ||
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[[Category: alpha helix]] | [[Category: alpha helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:16:17 2008'' |
Revision as of 14:16, 15 February 2008
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ATP Synthase b Subunit Dimerization Domain
Overview
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 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]. Active as Iron-chelate-transporting ATPase, with EC number 3.6.3.34 Full crystallographic information is available from OCA.
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:12022893
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