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Oleidesulfovibrio alaskensis
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x * 29000, recombinant enzyme, SDS-PAGE
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Oleidesulfovibrio alaskensis G20
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x * 29000, recombinant enzyme, SDS-PAGE
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homodimer
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ModB is the integral membrane protein
homodimer
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ModB is the integral membrane protein
homohexamer
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6 * 8100, SDS-PAGE, recombinant enzyme
homohexamer
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6 * 8100, SDS-PAGE, recombinant enzyme
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monomer
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additional information
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ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
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ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
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archaeal ModA proteins possess octahedral coordination, structure of the ModAB2C2 complex, overview. A single ModA protein with the molybdate oxyanion bound to the external side of a ModB2C2 complex. Molybdate or tungstate oxyanions are bound in a cleft between two lobes in ModA. Both lobes interact with ModB and there are several charged residues localized on the interface
additional information
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the enzyme components afModBC have 12 transmembrane alpha-helices that adopt the characteristic fold of type I ABC importers
additional information
the enzyme components afModBC have 12 transmembrane alpha-helices that adopt the characteristic fold of type I ABC importers
additional information
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ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
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bacterial ModA proteins possess tetrahedral coordination
additional information
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ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
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ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
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molybdenum is typically transported into the cell via an ABC type transport system encoded by the modABC operon. The modA gene codes for the periplasmic binding protein, modB codes for the transmembrane protein, and modC codes for an ATP-binding protein. Campylobacter jejuni encodes an uncharacterized molybdenum transport system including modABC in addition to a unique gene Cj0302c with unknown function
additional information
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ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
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the ModB protein has a molecular weight of 24000 Da, the ModC protein has a calculated molecular weight of 39045 Da
additional information
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ModA is the periplasmic molybdate-binding protein, ModC is a ATP-binding protein
additional information
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bacterial ModA proteins possess tetrahedral coordination
additional information
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ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
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structure of MolA falls into the cluster A of a class III periplasmic binding protein with two topologically similar globular domains, domain I and II correspond to residues 1-175 and 197-322, respectively, MolA topology and binding coordination, overview
additional information
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the 20 transmembrane alpha-helices of enzyme components hiMolBC present a type II fold
additional information
the 20 transmembrane alpha-helices of enzyme components hiMolBC present a type II fold
additional information
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ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
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ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
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ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
the regulatory domains of the nucleotide-binding pockets are in close contact and provide two oxyanion pockets at the shared interface, structure analysis and comparison
additional information
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the regulatory domains of the nucleotide-binding pockets are in close contact and provide two oxyanion pockets at the shared interface, structure analysis and comparison
additional information
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archaeal ModA proteins possess octahedral coordination, structure of the ModABC complex, overview
additional information
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ModABC consists of the ModA periplasmic solute-binding protein, the integral membrane-transport protein ModB and the ATP-binding and hydrolysis cassette protein ModC. Bilobal domain structure of ModA with two mixed alpha/beta domains linked by a hinge region and with a deep cleft between the two domains. Upon binding ligand one domain is rotated towards the other by a hinge-bending motion analogously to the Venus flytrap model of bacterial-type periplasmic binding proteins
additional information
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ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
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ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
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ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
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ModA is the periplasmic molybdate-binding protein, ModC is a ATP-binding protein
additional information
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ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
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ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
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ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
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ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
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archaeal ModA proteins possess octahedral coordination
additional information
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additional information
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ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
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ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
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bacterial ModA proteins possess tetrahedral coordination
additional information
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binding protein ModA of the molybdate transport system is a lipoprotein, ModB is a integral membrane, channel-forming protein, ModC is the ATP-binding energizer
additional information
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ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
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ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
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ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
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ModA is the periplasmic molybdate-binding protein, ModB is the integral membrane protein, ModC is a ATP-binding protein
additional information
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bacterial ModA proteins possess tetrahedral coordination