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

Masao Yamashita; Mark Shepherd; Wesley I. Booth; Hua Xie; Vincent Postis; Yvonne Nyathi; Svetomir B. Tzokov; Robert K, Poole; Stephen A. Baldwin; Per A. Bullough

doi:10.1074/jbc.M114.590414

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

Masao Yamashita, Mark Shepherd, Wesley I. Booth, Hua Xie, Vincent Postis, Yvonne Nyathi, Svetomir B. Tzokov, Robert K, Poole, Stephen A. Baldwin, Per A. Bullough

Drug Discovery Unit

Research output: Contribution to journal › Article › peer-review

15 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	23177-23188
Number of pages	12
Journal	Journal of Biological Chemistry
Volume	289
Issue number	33
DOIs	https://doi.org/10.1074/jbc.M114.590414
Publication status	Published - Aug 2014

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Yamashita, M., Shepherd, M., Booth, W. I., Xie, H., Postis, V., Nyathi, Y., Tzokov, S. B., Poole, R. K., Baldwin, S. A., & Bullough, P. A. (2014). Structure and function of the bacterial heterodimeric ABC transporter CydDC: stimulation of ATPase activity by thiol and heme compounds. Journal of Biological Chemistry, 289(33), 23177-23188. https://doi.org/10.1074/jbc.M114.590414

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abstract = "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.",

author = "Masao Yamashita and Mark Shepherd and Booth, {Wesley I.} and Hua Xie and Vincent Postis and Yvonne Nyathi and Tzokov, {Svetomir B.} and Poole, {Robert K,} and Baldwin, {Stephen A.} and Bullough, {Per A.}",

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doi = "10.1074/jbc.M114.590414",

language = "English",

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Yamashita, M, Shepherd, M, Booth, WI, Xie, H, Postis, V, Nyathi, Y, Tzokov, SB, Poole, RK, Baldwin, SA & Bullough, PA 2014, 'Structure and function of the bacterial heterodimeric ABC transporter CydDC: stimulation of ATPase activity by thiol and heme compounds', Journal of Biological Chemistry, vol. 289, no. 33, pp. 23177-23188. https://doi.org/10.1074/jbc.M114.590414

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 -

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

Abstract

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