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Showing 1–12 of 12 results
Advanced filters: Author: "Martin Caffrey" Clear advanced filters

  • This study presents the crystal structures of three functional forms of diacylglycerol kinase, an integral membrane protein that catalyses a crucial step in oligosaccharide and lipopolysaccharide synthesis and assembly; these X-ray structures are markedly different from the only other structure available for this unique kinase that was solved using solution NMR.

    • Dianfan Li
    • Joseph A. Lyons
    • Martin Caffrey
    Research
    Nature
    Volume: 497, P: 521-524

  • In Gram-positive bacteria, lipoprotein intramolecular transacylase Lit produces a lipoprotein variant with less immunogenicity. As such, Lit can be viewed as a virulence factor. Here, structural and functional characterization of the enzyme provides insight into its catalytic mechanism, setting the stage for future studies of Lit as a target for new antibiotics.

    • Samir Olatunji
    • Katherine Bowen
    • Martin Caffrey
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-14

  • The enzyme LspA from the human pathogen Staphylococcus aureus (MRSA) contributes to the integrity and function of the bacterial cell envelope. Here, authors provide crystal structures of LspA in complex with two natural antibiotics, which have profoundly different structures but inhibit LspA in an identical way.

    • Samir Olatunji
    • Xiaoxiao Yu
    • Martin Caffrey
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-11

  • Lipoproteins are essential components of bacterial membranes. Here the authors present the crystal structures ofPseudomonas aeruginosa and Escherichia coliapolipoprotein N-acyltransferase, which catalyses the final step in the lipoprotein synthesis pathway, and give insights into its mechanism.

    • Maciej Wiktor
    • Dietmar Weichert
    • Martin Caffrey
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-13

  • Diacylglycerol kinase is a small bacterial membrane-bound trimer that catalyses diacylglycerol conversion to phosphatidic acid. Here, the authors solve the crystal structure of the kinase bound to a lipid substrate and an ATP analogue, and show that the active site arose through convergent evolution.

    • Dianfan Li
    • Phillip J. Stansfeld
    • Martin Caffrey
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-12

  • Bacterial cell wall components are assembled in a transmembrane cycle that involves the membrane integral pyrophosphorylase, BacA. Here the authors solve the crystal structure of BacA which shows an interdigitated inverted topology repeat that hints towards a flippase function for BacA.

    • Meriem El Ghachi
    • Nicole Howe
    • Martin Caffrey
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-13

  • The X-ray crystal structure of the human β2 adrenergic receptor, a G-protein-coupled receptor (GPCR), covalently bound to a small-molecule agonist is solved. Comparison of this structure with structures of this GPCR in an inactive state and in an antibody-stabilized active state reveals how binding events at both the extracellular and intracellular surfaces stabilize the active conformation of the receptor. Molecular dynamics simulations suggest that the agonist-bound active state spontaneously relaxes to an inactive-like state in the absence of a G protein.

    • Daniel M. Rosenbaum
    • Cheng Zhang
    • Brian K. Kobilka
    Research
    Nature
    Volume: 469, P: 236-240

  • Huang et al. report a fully automated method for collecting and merging data from thousands of in meso-grown microcrystals. This in situ approach provides a fast and efficient way to determine the structures of membrane proteins from fragile microcrystals.

    • Chia-Ying Huang
    • Vincent Olieric
    • Meitian Wang
    ResearchOpen Access
    Communications Biology
    Volume: 1, P: 1-8

  • The lipid cubic phase (in meso) method is used for generating crystals and X-ray structures of integral membrane proteins. This protocol describes the cubicon method for concentrating membrane proteins in the cubic mesophase.

    • Pikyee Ma
    • Dietmar Weichert
    • Martin Caffrey
    Protocols
    Nature Protocols
    Volume: 12, P: 1745-1762