msbA Antibody

1. The ABC exporter MsbA can couple ATP hydrolysis to an adenylate kinase activity, where ADP is converted into AMP and ATP. Single-point mutations reveal that both ATPase and adenylate kinase mechanisms are associated with the same conserved motifs of the nucleotide-binding domain. PMID: 28004795
2. Data show that the conformational space of lipid ABC transporter MsbA changes upon vanadate trapping. PMID: 29069570
3. Data show that the twisting motion of ATP-binding cassette transporter MsbA plays an important role for the rearrangement of transmembrane helices and the opening of transmembrane domains on the periplasmic side. PMID: 26148303
4. Data indicate that E208A mutation interrupts the inward- to outward-facing conformational switch in ATP-binding cassette transport protein MsbA. PMID: 23306205
5. Data show that the isolated MsbA nucleotide-binding domain hydrolyzed ATP with V(max) = 45 nmol mg(-1) min(-1), similar to the full-length transporter. PMID: 22593573
6. Catalytic activity of MsbA reconstituted in nanodisc particles is modulated by remote interactions with the bilayer PMID: 22020218
7. analysis of the E506Q and H537A dysfunctional mutants in the E. coli ABC transporter MsbA PMID: 21462989
8. investigation of catalytic mechanism using mutants: L511P prevents effective ATP hydrolysis; D512G hydrolyzes ATP at rate 3-fold faster than wild type; both mutants bind ATP at near-wild-type levels but are unable to maintain cell viability PMID: 21344946
9. This is the first report of a direct measurement of lipid flippase activity of purified MsbA in a reconstituted system. PMID: 20412049
10. result suggests that deletion of the C-terminal alpha-helices may play a role in facilitating the outward-facing nucleotide-bound crystal structure of EcMsbA. PMID: 20179345
11. MsbA facilitates the rapid translocation of some lipids from the cytoplasmic to the periplasmic side of the inner membrane in living cells PMID: 15304478
12. spin-labeling & electron paramagnetic resonance spectroscopy used to characterize the conformational motion coupling energy expenditure to substrate translocation; results establish the structural dynamic basis of the power stroke in MDR ABC transporters PMID: 15890883
13. Lipopolysaccharide stabilizes the crystal packing of the ABC transporter MsbA PMID: 16511120
14. the LSGGQ NBD consensus sequence is consistent with an alpha-helical conformation and that these residues maintain extensive tertiary contacts throughout hydrolysis PMID: 17029409
15. Comparison among 4 x-ray structures of MsbA, trapped in different conformations (2 nucleotide-bound structures & 2 without nucleotide) reveals a flexible hinge formed by extracellular loops 2 & 3, allowing large ranges of motion PMID: 18024585
16. Proline to serine substitutions at either residue 18 or 50 of MsbA relieved the Kdo growth dependence observed in the isogenic wild-type strain. PMID: 18093093
17. analysis of the specific residues in these conserved ABC motifs within MsbA indicates that closure of the dimer interface does not occur upon ATP binding in this transporter. PMID: 19053284
18. MsbA can act as multidrug transporter, consistent with its structural similarities with the human multidrug resistance P-glycoprotein ABCB1, and transmembrane helix 6 plays an important role in the binding and transport of multiple drugs. PMID: 18803398

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KEGG: ecj:JW0897

STRING: 316385.ECDH10B_0984