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7.6.2.9: ABC-type quaternary amine transporter

This is an abbreviated version!
For detailed information about ABC-type quaternary amine transporter, go to the full flat file.

Word Map on EC 7.6.2.9

Reaction

ATP
+
H2O
 +
quaternary amine-[quaternary amine-binding protein][side 1]
=
ADP
 +
phosphate
 +
quaternary amine[side 2]
 +
[quaternary amine-binding protein][side 1]

Synonyms

ABC transporter, BetTA.halophytica, EC 3.6.3.32, glycine betaine porter II, glycine betaine transport system permease protein, glycine betaine transporter membrane protein, glycine betaine-binding protein, glycine betaine-binding protein OpuAC, glycine betaine/carnitine/choline-binding protein, glycine/betaine ABC transporter, N288_21505, N288_21525, N288_25665, OpuA, OpuAB, OpuAC, OpuB, OpuBC, OpuC, OpuCC, OpuD, OpuF, OpuF transporter, proline/betaine ABC transporter permease, ProU, proW, Quaternary-amine-transporting ATPase

ECTree

     7 Translocases
         7.6 Catalysing the translocation of other compounds
             7.6.2 Linked to the hydrolysis of a nucleoside triphosphate
                7.6.2.9 ABC-type quaternary amine transporter

Crystallization

Crystallization on EC 7.6.2.9 - ABC-type quaternary amine transporter

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
OpuBC protein crystal structure analysis, PDB ID 3R6U
U5LFB4; U5LHK3; U5LHN4
by hanging-drop method, structures of substrate-binding domain in complex with glycine betaine solved at 2.0 A resolution and in complex with glycine proline at 2.8 A resolution, structures show a substrate-binding protein-dependent-typical class II fold, structural differences of complexes occur within the ligand-binding pocket as well as across the domain-domain interface, explaining the differences in affinity of the substrate-binding domain-glycine betaine complex with KD = 0.017 mM, and substrate-binding domain-proline betaine complex with KD = 0.295 mM
-
OpuBC protein crystal structure analysis, PDB ID 3R6U
substrate-binding domain in complex with glycine betaine solved at 2.0 A resolution and in complex with glycine proline at 2.8 A resolution
-
substrate-binding protein OpuBC in complex with choline, to 1.6 A resolution. The positively charged trimethylammonium head group of choline is wedged into an aromatic cage formed by four tyrosine residues and is bound via cation-pi interactions. The hydroxyl group of choline protrudes out of this aromatic cage and makes a single interaction with residue Gln19. A water network stabilizes choline within its substrate-binding site and promotes indirect interactions between the two lobes of the OpuBC protein. Disruption of this intricate water network strongly reduces choline binding affinity or abrogates ligand binding
substrate-binding protein OpuCC in the apo-form and in complex with carnitine, glycine betaine, choline and ectoine to 2.3, 2.7, 2.4, 1.9 and 2.1 A resolution, respectively. OpuCC is composed of two alpha/beta/alpha globular sandwich domains linked by two hinge regions, with a substrate-binding pocket located at the interdomain cleft. Upon substrate binding, the two domains shift towards each other to trap the substrate
crystallization in an open and closed-liganded conformation, to 1.9 and 2.3 A resolution, respectively. Solutes like proline and carnitine bind with affinities that are 3 to 4 orders of magnitude lower than affinities of substrates glycine betaine or proline betaine. The low affinity substrates are not noticeably transported by membrane-reconstituted OpuA. The binding pocket is formed by three tryptophans coordinating the quaternary ammonium group of glycine betaine in the closed-liganded structure