Structure and function of the bacterial heterodimeric ABC transporter CydDC: stimulation of ATPase activity by thiol and heme compounds

TY - JOUR

T1 - Structure and function of the bacterial heterodimeric ABC transporter CydDC

T2 - stimulation of ATPase activity by thiol and heme compounds

AU - Yamashita, Masao

AU - Shepherd, Mark

AU - Booth, Wesley I.

AU - Xie, Hua

AU - Postis, Vincent

AU - Nyathi, Yvonne

AU - Tzokov, Svetomir B.

AU - Poole, Robert K,

AU - Baldwin, Stephen A.

AU - Bullough, Per A.

PY - 2014/8

Y1 - 2014/8

N2 - Background: The ABC transporter CydDC, which pumps sulfur compounds, is required for assembly of the bacterial respiratory machinery. Results: ATP hydrolysis by CydCD in response to sulfur compounds is modulated by hemes. Conclusion: Hemes regulate CydDC in pumping sulfur compounds. Significance: This work is a first step in understanding the structure, function, and regulation of a protein vital to the assembly of the respiratory machinery.

AB - Background: The ABC transporter CydDC, which pumps sulfur compounds, is required for assembly of the bacterial respiratory machinery. Results: ATP hydrolysis by CydCD in response to sulfur compounds is modulated by hemes. Conclusion: Hemes regulate CydDC in pumping sulfur compounds. Significance: This work is a first step in understanding the structure, function, and regulation of a protein vital to the assembly of the respiratory machinery.

UR - http://europepmc.org/abstract/med/24958725

U2 - 10.1074/jbc.M114.590414

DO - 10.1074/jbc.M114.590414

M3 - Article

C2 - 24958725

SN - 0021-9258

VL - 289

SP - 23177

EP - 23188

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 33

ER -