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Structure-basedmechanism forNa+/melibiose symportby MelB A.S. EthayathullaMohammad S. YousefAnowarul Amin2014 год

Structure-based mechanism for Na+/melibiose symport by MelB
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Аннотация: The bacterial melibiose permease (MelB) belongs to the glycoside–pentoside–hexuronide:cation symporter family, a part of the major facilitator superfamily (MFS). Structural information regarding glycoside–pentoside–hexuronide:cation symporter family transporters and other Na+-coupled permeases within MFS has been lacking, although a wealth of biochemical and biophysical data are available. Here we present the three-dimensional crystal structures of Salmonella typhimurium MelBSt in two conformations, representing an outward partially occluded and an outward inactive state of MelBSt. MelB adopts a typical MFS fold and contains a previously unidentified cation-binding motif. Three conserved acidic residues form a pyramidal-shaped cation-binding site for Na+, Li+ or H+, which is in close proximity to the sugar-binding site. Both cosubstrate-binding sites are mainly contributed by the residues from the amino-terminal domain. These two structures and the functional data presented here provide mechanistic insights into Na+/melibiose symport. We also postulate a structural foundation for the conformational cycling necessary for transport catalysed by MFS permeases in general. The bacterial symporter MelB transports galactosides with Na+, Li+ or H+ ions. Ethayathulla et al. present crystal structures of MelB in two distinct conformations, providing the first structural insights into the transport mechanism of a sodium-coupled permease of the major facilitator superfamily.
Год издания: 2014
Авторы: A.S. Ethayathulla, Mohammad S. Yousef, Anowarul Amin, Gérard Leblanc, H. Ronald Kaback, Lan Guan
Издательство: Nature Portfolio
Источник: Nature Communications
Ключевые слова: Bacterial Genetics and Biotechnology, Legume Nitrogen Fixing Symbiosis, Neonatal Health and Biochemistry
Другие ссылки: Nature Communications (PDF)
Nature Communications (HTML)
eScholarship (California Digital Library) (PDF)
eScholarship (California Digital Library) (HTML)
PubMed Central (HTML)
Europe PMC (PubMed Central) (PDF)
Europe PMC (PubMed Central) (HTML)
PubMed (HTML)