Closure of the cytoplasmic gate formed by TM5 and TM11 during transport in the oxalate/formate exchanger from Oxalobacter formigenes

Biochemistry

Volumn 53, Issue 49, 2014, Pages 7735-7744

  Iyalomhe, Osigbemhe ^a   Herrick, Dawn Z ^b   Cafiso, David S ^b   Maloney, Peter C ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF VIRGINIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CARBOXYLATION; POPULATION STATISTICS; SUBSTRATES;

CONFORMATIONAL EQUILIBRIUM; CONFORMATIONAL HETEROGENEITY; DISTANCE DISTRIBUTIONS; EPR MEASUREMENTS; HOMOLOGY MODELING; MAJOR FACILITATOR SUPERFAMILY; METHANETHIOSULFONATE; TRANSPORT PATHWAYS;

OXALIC ACID;

CARBOXYLIC ACID; CYSTEINE; MEMBRANE PROTEIN; METHANETHIOSULFONATE ETHYL CARBOXYLATE; OXALATE FORMATE EXCHANGER; TM11 PROTEIN; TM5 PROTEIN; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CARRIER PROTEIN; CROSS LINKING REAGENT; DYES, REAGENTS, INDICATORS, MARKERS AND BUFFERS; LIPOSOME; MESYLIC ACID DERIVATIVE; MUTANT PROTEIN; OXALIC ACID; OXLT PROTEIN, BACTERIA; RECOMBINANT PROTEIN; SPIN LABELING;

ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CYTOPLASM; ELECTRON SPIN RESONANCE; ENZYME MECHANISM; ENZYME SUBSTRATE; NONHUMAN; OXALOBACTER FORMIGENES; PREDICTION; PROTEIN CROSS LINKING; PROTEIN INTERACTION; PROTEIN MOTIF; PROTEIN STRUCTURE; PROTEIN TRANSPORT; SPIN LABELING; AMINO ACID SUBSTITUTION; ANTAGONISTS AND INHIBITORS; CHEMICAL STRUCTURE; CHEMISTRY; DRUG EFFECTS; GENETICS; KINETICS; METABOLISM; PROTEIN CONFORMATION; PROTEIN DOMAIN; TRANSPORT AT THE CELLULAR LEVEL;

OXALOBACTER FORMIGENES;

AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; BIOLOGICAL TRANSPORT; CROSS-LINKING REAGENTS; CYTOPLASM; ELECTRON SPIN RESONANCE SPECTROSCOPY; INDICATORS AND REAGENTS; KINETICS; LIPOSOMES; MEMBRANE TRANSPORT PROTEINS; MESYLATES; MODELS, MOLECULAR; MUTANT PROTEINS; OXALIC ACID; OXALOBACTER FORMIGENES; PERIPLASM; PROTEIN CONFORMATION; PROTEIN INTERACTION DOMAINS AND MOTIFS; RECOMBINANT PROTEINS; SPIN LABELS;

EID: 84918496432     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi5012173     Document Type: Article

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