Crystal structure of AqpZ tetramer reveals two distinct Arg-189 conformations associated with water permeation through the narrowest constriction of the water-conducting channel

Journal of Biological Chemistry

Volumn 281, Issue 1, 2006, Pages 454-460

  Jiang, Jiansheng ^a   Daniels, Brenda V ^a   Fu, Dax ^a  

^a BROOKHAVEN NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; CARRIER CONCENTRATION; CONFORMATIONS; ESCHERICHIA COLI; HYDROGEN BONDS; MONOMERS;

AQPZ TETRAMER; ARG-189 GUANIDINO GROUP; CARBONYL OXYGEN; WATER-CONDUCTING CHANNEL;

CRYSTAL STRUCTURE;

AQUAGLYCEROPORIN; ARGININE; CARBONYL DERIVATIVE; GUANIDINE DERIVATIVE; PROTEIN AQPZ; TETRAMER; THREONINE; UNCLASSIFIED DRUG; AQPZ PROTEIN, E COLI; AQUAPORIN; ESCHERICHIA COLI PROTEIN; MEMBRANE PROTEIN; WATER;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; CYTOPLASM; HYDROGEN BOND; HYDROPHILICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; WATER FLOW; WATER PERMEABILITY; CHEMISTRY; CRYSTALLOGRAPHY; ESCHERICHIA COLI; METABOLISM; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; TRANSPORT AT THE CELLULAR LEVEL;

ESCHERICHIA COLI;

AQUAPORINS; BIOLOGICAL TRANSPORT; CRYSTALLOGRAPHY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MEMBRANE PROTEINS; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; WATER;

EID: 33644850534     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M508926200     Document Type: Article

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