Journal
JOURNAL OF STRUCTURAL BIOLOGY
Volume 197, Issue 3, Pages 350-353Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2017.01.002
Keywords
ATPase; Membrane protein; Cryo-EM; Antibodies
Funding
- National Health and Medical Research Council Fellowship [APP1090408]
- National Health and Medical Research Council Fellowships [APP1004620, APP1109961.]
- National Health and Medical Research Council [APP1022143, APP1047004.]
- Singapore Ministry of Education Academic Research Fund Tier 3 [M0E2012-T3-1-001]
- Nanyang Structural Biology Institute, NTU, Singapore.
- Australian Research Council Fellowship [DE160100608.]
- Australian Research Council [DE160100608] Funding Source: Australian Research Council
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The bacterial A/V-type ATPase/synthase rotary motor couples ATP hydrolysis/synthesis with proton translocation across biological membranes. The A/V-type ATPase/synthase from Thermus thermophilus has been extensively studied both structurally and functionally for many years. Here we provide an 8.7 A resolution cryo-electron microscopy 3D reconstruction of this complex bound to single-domain antibody fragments, small monomeric antibodies containing just the variable heavy domain. Docking of known structures into the density revealed the molecular orientation of the domain antibodies, suggesting that structure determination of co-domain antibody:protein complexes could be a useful avenue for unstable or smaller proteins. Although previous studies suggested that the presence of fluoroaluminate in this complex could change the rotary state of this enzyme, we observed no gross structural rearrangements under these conditions. (C) 2017 Elsevier Inc. All rights reserved.
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