Structure of Mycobacterium tuberculosis mtFabD, a malonyl-CoA:acyl carrier protein transacylase (MCAT)

Hemza Ghadbane; Alistair K Brown; Laurent Kremer; Gurdyal S Besra; Klaus Fütterer

doi:10.1107/S1744309107042455

Structure of Mycobacterium tuberculosis mtFabD, a malonyl-CoA:acyl carrier protein transacylase (MCAT)

Hemza Ghadbane, Alistair K Brown, Laurent Kremer, Gurdyal S Besra, Klaus Fütterer

Biosciences

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

11 Citations (Scopus)

Abstract

Mycobacteria display a unique and unusual cell-wall architecture, central to which is the membrane-proximal mycolyl-arabinogalactan-peptidoglycan core (mAGP). The biosynthesis of mycolic acids, which form the outermost layer of the mAGP core, involves malonyl-CoA:acyl carrier protein transacylase (MCAT). This essential enzyme catalyses the transfer of malonyl from coenzyme A to acyl carrier protein AcpM, thus feeding these two-carbon units into the chain-elongation cycle of the type II fatty-acid synthase. The crystal structure of M. tuberculosis mtFabD, the mycobacterial MCAT, has been determined to 3.0 A resolution by multi-wavelength anomalous dispersion. Phasing was facilitated by Ni2+ ions bound to the 20-residue N-terminal affinity tag, which packed between the two independent copies of mtFabD.

Original language	English
Pages (from-to)	831-5
Number of pages	5
Journal	Acta Crystallographica Section F Structural Biology and Crystallization Communications
Volume	63
Issue number	10
DOIs	https://doi.org/10.1107/S1744309107042455
Publication status	Published - 1 Oct 2007

Keywords

mtFabD
malonyl-CoA:acyl carrier protein transacylases

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1107/S1744309107042455

Cite this

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title = "Structure of Mycobacterium tuberculosis mtFabD, a malonyl-CoA:acyl carrier protein transacylase (MCAT)",

abstract = "Mycobacteria display a unique and unusual cell-wall architecture, central to which is the membrane-proximal mycolyl-arabinogalactan-peptidoglycan core (mAGP). The biosynthesis of mycolic acids, which form the outermost layer of the mAGP core, involves malonyl-CoA:acyl carrier protein transacylase (MCAT). This essential enzyme catalyses the transfer of malonyl from coenzyme A to acyl carrier protein AcpM, thus feeding these two-carbon units into the chain-elongation cycle of the type II fatty-acid synthase. The crystal structure of M. tuberculosis mtFabD, the mycobacterial MCAT, has been determined to 3.0 A resolution by multi-wavelength anomalous dispersion. Phasing was facilitated by Ni2+ ions bound to the 20-residue N-terminal affinity tag, which packed between the two independent copies of mtFabD.",

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AU - Ghadbane, Hemza

AU - Brown, Alistair K

AU - Kremer, Laurent

AU - Besra, Gurdyal S

AU - Fütterer, Klaus

PY - 2007/10/1

Y1 - 2007/10/1

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AB - Mycobacteria display a unique and unusual cell-wall architecture, central to which is the membrane-proximal mycolyl-arabinogalactan-peptidoglycan core (mAGP). The biosynthesis of mycolic acids, which form the outermost layer of the mAGP core, involves malonyl-CoA:acyl carrier protein transacylase (MCAT). This essential enzyme catalyses the transfer of malonyl from coenzyme A to acyl carrier protein AcpM, thus feeding these two-carbon units into the chain-elongation cycle of the type II fatty-acid synthase. The crystal structure of M. tuberculosis mtFabD, the mycobacterial MCAT, has been determined to 3.0 A resolution by multi-wavelength anomalous dispersion. Phasing was facilitated by Ni2+ ions bound to the 20-residue N-terminal affinity tag, which packed between the two independent copies of mtFabD.

KW - mtFabD

KW - malonyl-CoA:acyl carrier protein transacylases

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JO - Acta Crystallographica Section F Structural Biology and Crystallization Communications

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IS - 10

ER -

Structure of Mycobacterium tuberculosis mtFabD, a malonyl-CoA:acyl carrier protein transacylase (MCAT)

Abstract

Keywords

UN SDGs

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