Improved model of proton pump crystal structure obtained by interactive molecular dynamics flexible fitting expands the mechanistic model for proton translocation in P-type ATPases

Frontiers in Physiology

Volumn 8, Issue APR, 2017, Pages

  Focht, Dorota ^a   Croll, Tristan I ^b   Pedersen, Bjorn P ^a   Nissen, Poul ^a  

^a AARHUS UNIVERSITY   (Denmark)

^b QUEENSLAND UNIVERSITY OF TECHNOLOGY   (Australia)

Author keywords

Arabidopsis thaliana AHA2; Crystallography; IMDFF; Membrane transport; Molecular dynamics; P type ATPases; Plasma membrane proton pump; Proton gradient

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATASE (CALCIUM); ADENOSINE TRIPHOSPHATASE (ZINC); ADENOSINE TRIPHOSPHATASE P TYPE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DEPROTECTION REACTION; HYDROGEN BOND; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; MOLECULAR STABILITY; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN STRUCTURE; PROTON TRANSPORT; SEQUENCE ALIGNMENT;

EID: 85018786458     PISSN: None     EISSN: 1664042X     Source Type: Journal    
DOI: 10.3389/fphys.2017.00202     Document Type: Article

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