Imperial College London
Alternate

Prof Steve Matthews

Faculty of Natural Sciences, Department of Life Sciences

Professor of Chemical and Structural Biology
 
 
 
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Contact

 

+44 (0)20 7594 5315s.j.matthews Website

 
 
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Location

 

602Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Darvill:2018:10.1016/j.str.2018.05.001,
author = {Darvill, N and Blake, T and Rouse, S and Hammoudi, P-M and Benjamin, S and Liu, B and Soldati-Favre, D and Matthews, S},
doi = {10.1016/j.str.2018.05.001},
journal = {Structure},
pages = {1059--1071.e6},
title = {Structural basis of phosphatidic acid sensing by APH in apicomplexan parasites},
url = {http://dx.doi.org/10.1016/j.str.2018.05.001},
volume = {26},
year = {2018}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Plasmodium falciparum and Toxoplasma gondii are obligate intracellular parasites that belong to the phylum of Apicomplexa and cause major human diseases. Their access to an intracellular lifestyle is reliant on the coordinated release of proteins from the specialized apical organelles called micronemes and rhoptries. A specific phosphatidic acid effector, the acylated pleckstrin homology domain-containing protein (APH) plays a central role in microneme exocytosis and thus is essential for motility, cell entry, and egress. TgAPH is acylated on the surface of the micronemes and recruited to phosphatidic acid (PA)-enriched membranes. Here, we dissect the atomic details of APH PA-sensing hub and its functional interaction with phospholipid membranes. We unravel the key determinant of PA recognition for the first time and show that APH inserts into and clusters multiple phosphate head-groups at the bilayer binding surface.
AU  - Darvill,N
AU  - Blake,T
AU  - Rouse,S
AU  - Hammoudi,P-M
AU  - Benjamin,S
AU  - Liu,B
AU  - Soldati-Favre,D
AU  - Matthews,S
DO  - 10.1016/j.str.2018.05.001
EP  - 1071
PY  - 2018///
SN  - 0969-2126
SP  - 1059
TI  - Structural basis of phosphatidic acid sensing by APH in apicomplexan parasites
T2  - Structure
UR  - http://dx.doi.org/10.1016/j.str.2018.05.001
UR  - http://hdl.handle.net/10044/1/59938
VL  - 26
ER  -
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