Backbone chemical shift assignments of the acyl-acyl carrier protein intermediates of the fatty acid biosynthesis pathway of Plasmodium falciparum

Upadhyay, Swati; Misra, Ashok; Surolia, Namita; Surolia, Avadhesha; Sundd, Monica

doi:10.1007/s12104-010-9212-2

Cited by 2 publications

(1 citation statement)

References 9 publications

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“…75 In P. falciparum acyl-ACP the hydrophobic cavity appears to be able to enclose up to a 12 carbon chain. 76,77 Insertion of the acyl chain induces a similar structural change to that seen in other carrier proteins, with helix III 0 moving away from helix II to enlarge the hydrophobic cavity as the acyl chain increases in length. MD simulations of b-hydroxydecanoyl-ACP suggested that substrate delivery was between a-helices II and III 0 .…”

Section: Acyl Acp Structuresmentioning

confidence: 78%

The structural role of the carrier protein – active controller or passive carrier

2012

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Common to all FASs, PKSs and NRPSs is a remarkable component, the acyl or peptidyl carrier protein (A/PCP). These take the form of small individual proteins in type II systems or discrete folded domains in the multi-domain type I systems and are characterized by a fold consisting of three major a-helices and between 60-100 amino acids. This protein is central to these biosynthetic systems and it must bind and transport a wide variety of functionalized ligands as well as mediate numerous protein-protein interactions, all of which contribute to efficient enzyme turnover. This review covers the structural and biochemical characterization of carrier proteins, as well as assessing their interactions with different ligands, and other synthase components. Finally, their role as an emerging tool in biotechnology is discussed.

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Section: Acyl Acp Structuresmentioning

confidence: 78%

The structural role of the carrier protein – active controller or passive carrier

2012

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Backbone and side chain 1H, 15N & 13C chemical shift assignments of the holo-acyl carrier protein (ACP) of Leishmania major

2012

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Acyl carrier protein (ACP) is a small acidic protein, an important cofactor involved in fatty acid biosynthesis. Its main function is to protect the growing acyl chain from the hydrophilic environment during fatty acid biosynthesis and simultaneously, present it to the active site of fatty acid pathway enzymes, liable for its elongation. The ACP molecule is expressed as apo-ACP (inactive) and is post-transitionally modified to the holo form (active) by the enzyme holo ACP synthase (ACPS). Here we report the complete backbone and side chain chemical shift assignments of the holo-ACP molecule of Leishmania major.

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Backbone chemical shift assignments of the acyl-acyl carrier protein intermediates of the fatty acid biosynthesis pathway of Plasmodium falciparum

Cited by 2 publications

References 9 publications

The structural role of the carrier protein – active controller or passive carrier

The structural role of the carrier protein – active controller or passive carrier

Backbone and side chain 1H, 15N & 13C chemical shift assignments of the holo-acyl carrier protein (ACP) of Leishmania major

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