I am working on the following projects at the moment:

• Lipoprotein Biogenesis Pathway
• LipID: Lipid Interactions with Membrane Proteins
• Twin Arginine Translocase
• KATP Potassium Channel
• Bacterial Chemotaxis
• Surface-Layer Proteins

One of the fundamental challenges in biological sciences is to visualise biomolecular machines in high-resolution detail. This is notoriously difficult, expensive and time-consuming to achieve by using experimental techniques, especially for proteins that exist in cell membranes, known as Integral membrane proteins (IMPs). These proteins play fundamental roles in cell biology e.g. as processing enzymes, ion channels, drug receptors, and solute transporters.

My group uses computational methods to study IMP structures and currently hosts MemProtMD; a pipeline for inserting experimentally-solved IMP structures into their native bilayer environment and analysing the stability, dynamics and resultant lipid interactions. This resource uses multiscale molecular dynamics (MD) simulations that permit the accurate assembly of an IMP into a membrane at the coarse-grain level, prior to careful assessment of the quality of the IMP structure at atomic resolution.

The MemProtMD pipeline also forms a springboard to studying the dynamics of experimentally solved structures through MD simulations. With the increasing threat of anti-microbial resistance, we are especially interested in bacterial IMPs. Knowledge of the three-dimensional structures of proteins involved in essential processes provides the physical details of potentially viable targets for killing drug-resistant, pathogenic bacteria. By breathing life into these frozen structures we may assess the association of proteins with lipids, drug molecules and other components of the protein complexes.

Phillip teaches the CH3F1 undergraduate module

I am supervising the following PhD students:

• Martin McAndrew (MRC DTP)
• Chelsea Brown (MRC DTP)
• Joshua Sauer (Oxford)
• Will Pipatpolkai (Oxford)
• Dan Quetschlich (Oxford/UCB)
• Patrick Simcock (Oxford/IBM)
• Michael Horrell (Oxford/UCB)

Please get in touch if you would like to join the team.

Journals

• von Kügelgen, Andriko, Tang, Haiping, Hardy, Gail G., Kureisaite-Ciziene, Danguole, Brun, Yves V., Stansfeld, Phillip J., Robinson, Carol V., Bharat, Tanmay A. M., 2020. In situ structure of an intact lipopolysaccharide-bound bacterial surface layer. Cell
• Burt, Alister, Cassidy, C. Keith, Ames, Peter, Bacia-Verloop, Maria, Baulard, Megghane, Huard, Karine, Luthey-Schulten, Zaida, Desfosses, Ambroise, Stansfeld, Phillip J., Margolin, William, Parkinson, John S., Gutsche, Irina, 2020. Complete structure of the chemosensory array core signalling unit in an E. coli 1 minicell strain. Nature Communications
• Pye, Valerie E., Rosa, Annachiara, Bertelli, Cinzia, Struwe, Weston B., Maslen, Sarah L., Corey, Robin A., Liko, Idlir, Hassall, Mark, Mattiuzzo, Giada, Ballandras-Colas, Allison, Nans, Andrea, Takeuchi, Yasuhiro, Stansfeld, Phillip J., Skehel, J. Mark, Robinson, Carol V., Pizzato, Massimo, Cherepanov, Peter, 2020. A bipartite structural organization defines the SERINC family of HIV-1 restriction factors. Nature Structural & Molecular Biology, 27, pp. 78-83
• Cassidy, Keith, Himes, Benjamin A., Sun, Dapeng, Ma, Jun, Zhao, Gongpu, Parkinson, John S., Stansfeld, Phillip J., Luthey-Schulten, Z., Zhang, Peijun, 2020. Structure and dynamics of the E. coli chemotaxis core signaling complex by cryo-electron tomography and molecular simulations. Communications Biology, 3 (24)
• Bushell, Simon R., Pike, Ashley C. W., Falzone, Maria E., Rorsman, Nils J. G., Ta, Chau M., Corey, Robin A., Newport, Thomas D., Christianson, John C., Scofano, Lara F., Shintre, Chitra A., Tessitore, Annamaria, Chu, Amy, Wang, Qinrui, Shrestha, Leela, Mukhopadhyay, Shubhashish M. M., Love, James D., Burgess-Brown, Nicola A., Sitsapesan, Rebecca, Stansfeld, Phillip J., Huiskonen, Juha T., Tammaro, Paolo, Accardi, Alessio, Carpenter, Elisabeth P., 2019. The structural basis of lipid scrambling and inactivation in the endoplasmic reticulum scramblase TMEM16K. Nature Communications, 10 (1)
• Rao, Shanlin, Klesse, Gianni, Stansfeld, Phillip J., Tucker, Stephen J., Sansom, Mark S. P., 2019. A heuristic derived from analysis of the ion channel structural proteome permits the rapid identification of hydrophobic gates. Proceedings of the National Academy of Sciences of the United States of America, 116 (28), pp. 13989-13995
• Rinné, Susanne, Kiper, Aytug K., Vowinkel, Kirsty S., Ramírez, David, Schewe, Marcus, Bedoya, Mauricio, Aser, Diana, Gensler, Isabella, Netter, Michael F., Stansfeld, Phillip J., Baukrowitz, Thomas, Gonzalez, Wendy, Decher, Niels, 2019. The molecular basis for an allosteric inhibition of K+-flux gating in K2P channels. eLife, 8
• Corey, Robin A., Vickery, Owen N., Sansom, Mark S. P., Stansfeld, Phillip J., 2019. Insights into membrane protein?lipid interactions from free energy calculations. Journal of Chemical Theory and Computation, 15 (10), pp. 5727-5736
• Parker, Joanne L., Corey, Robin A., Stansfeld, Phillip J., Newstead, Simon, 2019. Structural basis for substrate speci?city and regulation of nucleotide sugar transporters in the lipid bilayer. Nature Communications, 10
• Parker, Joanne L., Corey, Robin A., Stansfeld, Phillip J., Newstead, Simon, 2019. Structural basis for substrate specificity and regulation of nucleotide sugar transporters in the lipid bilayer. Nature Communications, 10 (1)
• Caffalette, Christopher A., Corey, Robin A., Sansom, Mark S. P., Stansfeld, Phillip J., Zimmer, Jochen, 2019. A lipid gating mechanism for the channel-forming O antigen ABC transporter. Nature Communications, 10 (1)
• Abraham, Mark, Apostolov, Rossen, Barnoud, Jonathan, Bauer, Paul, Blau, Christian, Bonvin, Alexandre M.J.J., Chavent, Matthieu, Chodera, John, Condic-Jurkic, Karmen, Delemotte, Lucie, Grubmüller, Helmut, Howard, Rebecca J., Jordan, E. Joseph, Lindahl, Erik, Ollila, O. H. Samuli, Selent, Jana, Smith, Daniel G. A., Stansfeld, Phillip J., Tiemann, Johanna K.S., Trellet, Mikael, Woods, Christopher, Zhmurov, Artem, 2019. Sharing data from molecular simulations. Journal of Chemical Information and Modeling, 59 (10), pp. 4093-4099
• Yamamoto, Eiji, Domanski,, Jan, Naughton, Fiona B., Best , Robert B., Kalli, Antreas C., Stansfeld, Phillip J., Sansom, Mark S. P., 2019. Multiple lipid binding sites determine the affinity of PH domains for phosphoinositide-containing membranes. Science Advances
• Ni, Tao, Jiao, Fang, Yu, Xiulian, Aden, Sa?a, Ginger, Lucy, Williams, Sophie, Bai, Fangfang, Pra?ák, Vojtech, Karia, Dimple, Stansfeld, Phillip J., Zhang, Peijun, Munson, George, Anderluh, Gregor, Scheuring, Simon, Gilbert, Robert J. C., 2019. Structure and mechanism of bactericidal mammalian perforin-2, an ancient agent of innate immunity. Science Advances
• Corey, Robin A., Stansfeld, Phillip J., Sansom, Mark S. P., 2019. The energetics of protein-lipid interactions as viewed by molecular simulations. Biochemical Society Transactions
• Bolla, Jani Reddy, Corey, Robin A., Sahin, Cagla, Gault, Joseph, Hummer, Alissa, Hopper, Jonathan T. S., Lane, David P., Drew, David, Allison, Timothy M., Stansfeld, Phillip J., Robinson, Carol V., Landreh, Michael, 2019. A mass spectrometry-based approach to distinguish annular and specific lipid binding to membrane proteins. Angewandte Chemie International Edition
• Autzen, Henriette E., Koldsø, Heidi, Stansfeld, Phillip J., Gourdon, Pontus, Sansom, Mark S. P., Nissen, Poul, 2018. Interactions of a bacterial Cu(I)-ATPase with a complex lipid environment. Biochemistry, 57 (28), pp. 4063-4073
• Chavent, Matthieu, Karia, Dimple, Kalli, Antreas C., Domanski, Jan, Duncan, Anna L., Hedger, George, Stansfeld, Phillip J., Seiradake, Elena, Jones, E. Yvonne, Sansom, Mark S. P., 2018. Interactions of the EphA2 kinase domain with PIPs in membranes : implications for receptor function. Structure, 26 (7), pp. 1025-1034.e2
• Liko, Idlir, Degiacomi, Matteo T., Lee, Sejeong, Newport, Thomas D., Gault, Joseph, Reading, Eamonn, Hopper, Jonathan T. S., Housden, Nicholas G., White, Paul, Colledge, Matthew, Sula, Altin, Wallace, B. A., Kleanthous, Colin, Stansfeld, Phillip J., Bayley, Hagan, Benesch, Justin L. P., Allison, Timothy M., Robinson, Carol V., 2018. Lipid binding attenuates channel closure of the outer membrane protein OmpF. Proceedings of the National Academy of Sciences of the United States of America, 115 (26), pp. 6691-6696
• Rao, Shanlin, Lynch, Charlotte I., Klesse, Gianni, Oakley, Georgia E., Stansfeld, Phillip J., Tucker, Stephen J., Sansom, Mark S. P., 2018. Water and hydrophobic gates in ion channels and nanopores. Faraday Discussions, 209, pp. 231-247
• Domanski, Jan, Sansom, Mark S. P., Stansfeld, Phillip J., Best, Robert B., 2018. Balancing force field protein?lipid interactions to capture transmembrane Helix?Helix association. Journal of Chemical Theory and Computation, 14 (3), pp. 1706-1715
• Newport, Thomas D., Sansom, Mark S. P., Stansfeld, Phillip J., 2018. The MemProtMD database : a resource for membrane-embedded protein structures and their lipid interactions. Nucleic Acids Research, 47 (D1), pp. D390-D397
• Ni, Tao, Williams, Sophie I., Rezelj, Sa?a, Anderluh, Gregor, Harlos, Karl, Stansfeld, Phillip J., Gilbert, Robert J. C., 2018. Structures of monomeric and oligomeric forms of the Toxoplasma gondiiperforin-like protein 1. Science Advances, 4 (3)
• El Ghachi, Meriem, Howe, Nicole, Huang, Chia-Ying, Olieric, Vincent, Warshamanage, Rangana, Touzé, Thierry, Weichert, Dietmar, Stansfeld, Phillip J., Wang, Meitian, Kerff, Fred, Caffrey, Martin, 2018. Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis. Nature Communications, 9 (1)

Further Publications