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Structural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA

Author

Listed:
  • David Albesa-Jové

    (Unidad de Biofísica, Consejo Superior de Investigaciones Científicas—Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC,UPV/EHU), Barrio Sarriena s/n
    Universidad del País Vasco
    IKERBASQUE, Basque Foundation for Science)

  • Zuzana Svetlíková

    (Faculty of Natural Sciences, Comenius University in Bratislava)

  • Montse Tersa

    (Unidad de Biofísica, Consejo Superior de Investigaciones Científicas—Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC,UPV/EHU), Barrio Sarriena s/n
    Universidad del País Vasco)

  • Enea Sancho-Vaello

    (Unidad de Biofísica, Consejo Superior de Investigaciones Científicas—Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC,UPV/EHU), Barrio Sarriena s/n
    Universidad del País Vasco)

  • Ana Carreras-González

    (Unidad de Biofísica, Consejo Superior de Investigaciones Científicas—Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC,UPV/EHU), Barrio Sarriena s/n
    Universidad del País Vasco)

  • Pascal Bonnet

    (Université d’Orléans et CNRS, ICOA, UMR 7311)

  • Pedro Arrasate

    (Unidad de Biofísica, Consejo Superior de Investigaciones Científicas—Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC,UPV/EHU), Barrio Sarriena s/n
    Universidad del País Vasco)

  • Ander Eguskiza

    (Unidad de Biofísica, Consejo Superior de Investigaciones Científicas—Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC,UPV/EHU), Barrio Sarriena s/n
    Universidad del País Vasco)

  • Shiva K. Angala

    (Mycobacteria Research Laboratories, Immunology and Pathology, Colorado State University)

  • Javier O. Cifuente

    (Unidad de Biofísica, Consejo Superior de Investigaciones Científicas—Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC,UPV/EHU), Barrio Sarriena s/n
    Universidad del País Vasco)

  • Jana Korduláková

    (Faculty of Natural Sciences, Comenius University in Bratislava)

  • Mary Jackson

    (Mycobacteria Research Laboratories, Immunology and Pathology, Colorado State University)

  • Katarína Mikušová

    (Faculty of Natural Sciences, Comenius University in Bratislava)

  • Marcelo E. Guerin

    (Unidad de Biofísica, Consejo Superior de Investigaciones Científicas—Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC,UPV/EHU), Barrio Sarriena s/n
    Universidad del País Vasco
    IKERBASQUE, Basque Foundation for Science
    Structural Biology Unit, CIC bioGUNE, Bizkaia Technology Park)

Abstract

The biosynthesis of phospholipids and glycolipids are critical pathways for virtually all cell membranes. PatA is an essential membrane associated acyltransferase involved in the biosynthesis of mycobacterial phosphatidyl-myo-inositol mannosides (PIMs). The enzyme transfers a palmitoyl moiety from palmitoyl–CoA to the 6-position of the mannose ring linked to 2-position of inositol in PIM1/PIM2. We report here the crystal structures of PatA from Mycobacterium smegmatis in the presence of its naturally occurring acyl donor palmitate and a nonhydrolyzable palmitoyl–CoA analog. The structures reveal an α/β architecture, with the acyl chain deeply buried into a hydrophobic pocket that runs perpendicular to a long groove where the active site is located. Enzyme catalysis is mediated by an unprecedented charge relay system, which markedly diverges from the canonical HX4D motif. Our studies establish the mechanistic basis of substrate/membrane recognition and catalysis for an important family of acyltransferases, providing exciting possibilities for inhibitor design.

Suggested Citation

  • David Albesa-Jové & Zuzana Svetlíková & Montse Tersa & Enea Sancho-Vaello & Ana Carreras-González & Pascal Bonnet & Pedro Arrasate & Ander Eguskiza & Shiva K. Angala & Javier O. Cifuente & Jana Kordul, 2016. "Structural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA," Nature Communications, Nature, vol. 7(1), pages 1-12, April.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms10906
    DOI: 10.1038/ncomms10906
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    Cited by:

    1. Shiva Kumar Angala & Ana Carreras-Gonzalez & Emilie Huc-Claustre & Itxaso Anso & Devinder Kaur & Victoria Jones & Zuzana Palčeková & Juan M. Belardinelli & Célia Sousa-d’Auria & Libin Shi & Nawel Slam, 2023. "Acylation of glycerolipids in mycobacteria," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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