1ijp

From Proteopedia

(Difference between revisions)

Revision as of 07:47, 3 July 2019

Solution Structure of Ala20Pro/Pro64Ala substituted subunit c of Escherichia coli ATP synthase

Structural highlights

1ijp is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1a91, 1c0v, 1c99
Activity:	H(+)-transporting two-sector ATPase, with EC number 3.6.3.14
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ATPL_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.[HAMAP-Rule:MF_01396] Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of 10 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.[HAMAP-Rule:MF_01396]

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 structure of the A20P/P64A mutated subunit c of Escherichia coli ATP synthase, in which the essential proline has been switched from residue 64 of the second transmembrane helix (TMH) to residue 20 of the first TMH, has been solved by (15)N,(1)H NMR in a monophasic chloroform/methanol/water (4:4:1) solvent mixture. The cA20P/P64A mutant grows as well as wild type, and the F(0)F(1) complex is fully functional in ATPase-coupled H(+) pumping. Residues 20 and 64 lie directly opposite to each other in the hairpin-like structure of wild type subunit c, and the prolinyl 64 residue is thought to induce a slight bend in TMH-2 such that it wraps around a more straightened TMH-1. In solution, the A20P/P64A substituted subunit c also forms a hairpin of two alpha-helices, with residues 41-45 forming a connecting loop as in the case of the wild type protein, but, in this case, Pro(20) induces a bend in TMH-1, which then packs against a more straightened TMH-2. The essential prolinyl residue, whether at position 64 or 20, lies close to the aspartyl 61 H(+) binding site. The prolinyl residue may introduce structural flexibility in this region of the protein, which may be necessary for the proposed movement of the alpha-helical segments during the course of the H(+) pumping catalytic cycle.

Structure of Ala(20) --> Pro/Pro(64) --> Ala substituted subunit c of Escherichia coli ATP synthase in which the essential proline is switched between transmembrane helices.,Dmitriev OY, Fillingame RH J Biol Chem. 2001 Jul 20;276(29):27449-54. Epub 2001 Apr 30. PMID:11331283^[1]

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

References

↑ Dmitriev OY, Fillingame RH. Structure of Ala(20) --> Pro/Pro(64) --> Ala substituted subunit c of Escherichia coli ATP synthase in which the essential proline is switched between transmembrane helices. J Biol Chem. 2001 Jul 20;276(29):27449-54. Epub 2001 Apr 30. PMID:11331283 doi:10.1074/jbc.M100762200

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/1ijp"

Categories: Large Structures | Dmitriev, O Y | Fillingame, R H | Hydrolase | Transmembrane helix

@@ Line 1: / Line 1: @@
 ==Solution Structure of Ala20Pro/Pro64Ala substituted subunit c of Escherichia coli ATP synthase==
-<StructureSection load='1ijp' size='340' side='right' caption='[[1ijp]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<StructureSection load='1ijp' size='340' side='right'caption='[[1ijp]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1ijp]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IJP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IJP FirstGlance]. <br>
@@ Line 14: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ij/1ijp_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ij/1ijp_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 31: / Line 31: @@
 ==See Also==
-*[[ATPase|ATPase]]
+*[[ATPase 3D structures|ATPase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Dmitriev, O Y]]
 [[Category: Fillingame, R H]]
 [[Category: Hydrolase]]
 [[Category: Transmembrane helix]]

1ijp

From Proteopedia

Revision as of 07:47, 3 July 2019

Solution Structure of Ala20Pro/Pro64Ala substituted subunit c of Escherichia coli ATP synthase

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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