Cd2+ and the N-terminal metal-binding domain protect the putative membranous CPC motif of the Cd2+-ATPase of Listeria monocytogenes.
about
The plant P1B-type ATPase AtHMA4 transports Zn and Cd and plays a role in detoxification of transition metals supplied at elevated levelsNovel Cadmium Resistance Determinant in Listeria monocytogenesStructural basis for metal binding specificity: the N-terminal cadmium binding domain of the P1-type ATPase CadA.A P-type ATPase importer that discriminates between essential and toxic transition metalsBacterial ATP-driven transporters of transition metals: physiological roles, mechanisms of action, and roles in bacterial virulence.The distinct roles of the N-terminal copper-binding sites in regulation of catalytic activity of the Wilson's disease protein.The N-terminal degenerated metal-binding domain is involved in the heavy metal transport activity of TaHMA2.Cd(2+) extrusion by P-type Cd(2+)-ATPase of Staphylococcus aureus 17810R via energy-dependent Cd(2+)/H(+) exchange mechanism.The cadmium transport sites of CadA, the Cd2+-ATPase from Listeria monocytogenes.In silico design and construction of metal-binding hybrid proteins for specific removal of cadmium based on CS3 pili display on the surface of Escherichia coli.Heavy metal transport by AtHMA4 involves the N-terminal degenerated metal binding domain and the C-terminal His11 stretch.A novel heavy metal ATPase peptide from Prosopis juliflora is involved in metal uptake in yeast and tobacco.
P2860
Q28304248-E0062F06-80DB-43ED-BCDE-074F9276F1CCQ36227038-947BCC85-28F6-4069-9E1A-6B9D46A29CE8Q36583819-FE7CF67C-C3CB-4798-9ABC-269CEE9CC976Q37118892-C3E0E58D-742E-4644-BFF7-EFB6C33CD8F3Q37928933-DC86BD10-E1E8-4185-8C2A-93C74710F8ADQ38353817-1B5B13EB-FFAD-44EB-A9FB-F56BAAA5E395Q40875658-93E31AF5-CFCC-45D9-9BF4-C26FDCF75D07Q42212259-69CA9377-61CC-4324-B0F5-0042A3260670Q42691139-6254D6EA-70AA-40FA-8B70-77C5A03B3125Q44842020-CAD6C7F6-9332-476E-A2D5-65E52D2FF675Q45284398-423C573C-2420-4E05-8954-3B8DE09EDF21Q46454521-0FEE45AA-B251-4C7E-9FA5-ABA5CF0E2D2D
P2860
Cd2+ and the N-terminal metal-binding domain protect the putative membranous CPC motif of the Cd2+-ATPase of Listeria monocytogenes.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
Cd2+ and the N-terminal metal- ...... ase of Listeria monocytogenes.
@en
Cd2+ and the N-terminal metal- ...... ase of Listeria monocytogenes.
@nl
type
label
Cd2+ and the N-terminal metal- ...... ase of Listeria monocytogenes.
@en
Cd2+ and the N-terminal metal- ...... ase of Listeria monocytogenes.
@nl
prefLabel
Cd2+ and the N-terminal metal- ...... ase of Listeria monocytogenes.
@en
Cd2+ and the N-terminal metal- ...... ase of Listeria monocytogenes.
@nl
P2093
P2860
P356
P1433
P1476
Cd2+ and the N-terminal metal- ...... ase of Listeria monocytogenes.
@en
P2093
Chen Chou Wu
Elisabeth Mintz
Florent Guillain
Nathalie Bal
Patrice Catty
P2860
P304
P356
10.1042/BJ20021416
P407
P577
2003-02-01T00:00:00Z