The paper determines the structure of the SIT1 proline transporter complexed with ACE2 using cryo-EM, revealing substrate specificity and structural changes related to transport and a disease-causing mutation.

bioRxiv · May 17, 2023Biophysics

The structural basis of fatty acid elongation by the ELOVL elongases

L. Nie, A. C. Pike, T. C. Pascoa, S. R. Bushell, A. Quigley, G. F. Ruda, A. Chu, V. Cole, D. Speedman, T. Moreira, L. Shrestha, S. M. Mukhopadhyay, N. A. Burgess-Brown, J. D. Love, P. E. Brennan, E. P. Carpenter

The paper reports the structure of the human ELOVL7 elongase, revealing its catalytic mechanism and substrate-binding sites, with implications for inhibiting VLCFA accumulation in diseases.

bioRxiv · Nov 11, 2020Biochemistry

The structural basis of lipid scrambling and inactivation in the endoplasmic reticulum scramblase TMEM16K

S. R. Bushell, A. C. W. Pike, M. E. Falzone, N. J. G. Rorsman, C. M. Ta, R. A. Corey, T. D. Newport, C. A. Shintre, A. Tessitore, A. Chu, Q. Wang, L. Shrestha, S. Mukhopadhyay, J. D. Love, N. A. Burgess-Brown, , E. P. Carpenter

This study identifies TMEM16K as an ER-resident calcium-regulated lipid scramblase and elucidates its structural basis for lipid scrambling and inactivation.

bioRxiv · Dec 12, 2018Biochemistry

Structures of DPAGT1 explain glycosylation disease mechanisms and advance TB antibiotic design

Y. Y. Dong, H. Wang, A. C. Pike, S. J. Cochrane, S. Hamedzade, F. J. Wyszynsk, S. R. Bushell, S. F. Royer, D. A. Widdick, A. Sajid, H. I. Boshoff, R. Lucas, W.-M. Liu, S. S. Lee, T. Machida, , E. P. Carpenter

This paper determines the structures of DPAGT1 with substrates and inhibitors, revealing catalytic mechanisms and disease-causing mutations, and designs non-toxic antibiotics for tuberculosis.

bioRxiv · Apr 2, 2018Biochemistry