NDLI: Aqueous access pathways in subunit a of rotary ATP synthase extend to both sides of the membrane

Content Provider	PubMed Central
Author	Angevine, Christine M. Herold, Kelly A. G. Fillingame, Robert H.
Copyright Year	2003
Abstract	The role of subunit a in promoting proton translocation and rotary motion in the Escherichia coli F1Fo ATP synthase is poorly understood. In the membrane-bound Fo sector of the enzyme, H+ binding and release occur at Asp-61 in the middle of the second transmembrane helix (TMH) of subunit c. Protons are thought to reach Asp-61 at the center of the membrane via aqueous channels formed at least in part by one or more of the five TMHs of subunit a. Aqueous access pathways have previously been mapped to surfaces of aTMH4. Here we have substituted Cys into the second and fifth TMHs of subunit a and carried out chemical modification with Ag+ and N-ethylmaleimide to define the aqueous accessibility of residues along these helices. Access to cAsp-61 at the center of the membrane may be mediated in part by Ag+-sensitive residues 248, 249, 251, and 252 in aTMH5. From the periplasmic surface, aqueous access to cAsp-61 may be mediated by silver-sensitive residues 115, 116, 119, 120, 122, and 126 in aTMH2. The Ag+-sensitive residues in TMH2, -4, and -5 form a continuum extending from the periplasmic to the cytoplasmic side of the membrane. In an arrangement of helices supported by second-site revertant and crosslinking analyses, these residues cluster at the interior of a four-helix bundle formed by TMH2–5. The aqueous access pathways at the interior of subunit a may be gated by a swiveling of helices in this bundle, alternately exposing cytoplasmic and periplasmic half channels to cAsp-61 during the H+ transport cycle.
Related Links	http://dx.doi.org/10.1073/pnas.2234364100
Ending Page	13183
Page Count	5
Starting Page	13179
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	23
Volume Number	100
Language	English
Publisher	National Academy of Sciences
Publisher Date	2003-11-11
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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Aqueous access pathways in subunit a of rotary ATP synthase extend to both sides of the membrane

Large conformational changes of the ɛ subunit in the bacterial F1F0 ATP synthase provide a ratchet action to regulate this rotary motor enzyme

Subunit a Facilitates Aqueous Access to a Membrane-embedded Region of Subunit c in Escherichia coli F1F0 ATP Synthase*

Subunit a Facilitates Aqueous Access to a Membrane-embedded Region of Subunit c in Escherichia coli F1F0 ATP Synthase

Subunit rotation of ATP synthase embedded in membranes: a or β subunit rotation relative to the c subunit ring

Aqueous Access Pathways in ATP Synthase Subunit a REACTIVITY OF CYSTEINE SUBSTITUTED INTO TRANSMEMBRANE HELICES 1, 3, AND 5

Rotation of the c subunit oligomer in fully functional F1Fo ATP synthase

The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10

Energy-driven subunit rotation at the interface between subunit a and the c oligomer in the FO sector of Escherichia coli ATP synthase

Aqueous access pathways in subunit a of rotary ATP synthase extend to both sides of the membrane

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