1l2p

From Proteopedia

(Difference between revisions)

Revision as of 12:18, 13 November 2019

ATP Synthase b Subunit Dimerization Domain

Structural highlights

1l2p is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. The December 2005 RCSB PDB Molecule of the Month feature on ATP Synthase by David S. Goodsell is 10.2210/rcsb_pdb/mom_2005_12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:	Iron-chelate-transporting ATPase, with EC number 3.6.3.34
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ATPF_ECOLI] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity).^[1] Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0) (By similarity).^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ McCormick KA, Cain BD. Targeted mutagenesis of the b subunit of F1F0 ATP synthase in Escherichia coli: Glu-77 through Gln-85. J Bacteriol. 1991 Nov;173(22):7240-8. PMID:1682301
↑ McCormick KA, Cain BD. Targeted mutagenesis of the b subunit of F1F0 ATP synthase in Escherichia coli: Glu-77 through Gln-85. J Bacteriol. 1991 Nov;173(22):7240-8. PMID:1682301
↑ Del Rizzo PA, Bi Y, Dunn SD, Shilton BH. The "second stalk" of Escherichia coli ATP synthase: structure of the isolated dimerization domain. Biochemistry. 2002 May 28;41(21):6875-84. PMID:12022893

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1l2p"

@@ Line 1: / Line 1: @@
 ==ATP Synthase b Subunit Dimerization Domain==
-<StructureSection load='1l2p' size='340' side='right' caption='[[1l2p]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
+<StructureSection load='1l2p' size='340' side='right'caption='[[1l2p]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1l2p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. The December 2005 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''ATP Synthase''  by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2005_12 10.2210/rcsb_pdb/mom_2005_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L2P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L2P FirstGlance]. <br>
@@ Line 28: / Line 28: @@
 </div>
 <div class="pdbe-citations 1l2p" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[ATPase 3D structures|ATPase 3D structures]]
 == References ==
 <references/>
@@ Line 35: / Line 38: @@
 [[Category: ATP Synthase]]
 [[Category: Iron-chelate-transporting ATPase]]
+[[Category: Large Structures]]
 [[Category: RCSB PDB Molecule of the Month]]
 [[Category: Bi, Y]]

1l2p

From Proteopedia

Revision as of 12:18, 13 November 2019

ATP Synthase b Subunit Dimerization Domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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