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CtpB is a plasma membrane copper (I) transporting P-type ATPase of Mycobacterium tuberculosis

机译:CtpB是运输结核分枝杆菌的P型ATPase的质膜铜(I)

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摘要

Topology, functional motifs, and domains of CtpB. The predicted topology of CtpB shows eight TM helices (1 to 8), locating the N- and C-terminal ends within the cytoplasmic portion. The cytoplasmic domains are represented by stitched lines and the functional motifs of P -type ATPase are shown. The amino acids responsible for cation coordination within TM segments 6, 7 and 8 are highlighted in bold. The TM helices were predicted using TOPCONS. The multiple alignment of the N-terminal end, TM6, TM7, and TM8 of CtpB and other bacterial characterized Cu -ATPases (CopA from ( ) and ( )) was constructed using Clustal Omega. Some of the amino acids involved in the coordination of Cu are located within TM6, 7 and 8. The residues are classified as nonpolar (black), polar (green), acid (blue), and basic (red)
机译:CtpB的拓扑结构,功能性基序和结构域。 CtpB的预测拓扑显示八个TM螺旋(1到8),位于细胞质部分的N和C末端。胞质结构域由缝合线表示,并且显示了P型ATP酶的功能基序。 TM段6、7和8中负责阳离子配位的氨基酸以粗体突出显示。 TM螺旋是使用TOPCONS预测的。使用Clustal Omega构建CtpB的N末端,TM6,TM7和TM8与其他细菌表征的Cu -ATPase(()和()中的CopA)的多重比对。与Cu配位有关的某些氨基酸位于TM6、7和8中。残基分为非极性(黑色),极性(绿色),酸(蓝色)和碱性(红色)。

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