Author

M. R. MacRae

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 2 Biophysics· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:protein structure prediction· 3 Assay:cryo-EM· 2 Organism:E. coli· 2 Organism:bacteria (other)· 1 Approach:deep learning· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1

Frequent Co-Authors

D. C. Ekiert· 4 shared G. Bhabha· 4 shared N. Coudray· 4 shared G. L. Isom· 3 shared L. R. Kolich· 2 shared C. Lam· 1 shared C. T. McManus· 1 shared D. Puvanendran· 1 shared

Activity by Year

2019-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 34 mutual co-author links

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4 shared papersBiochemistry

D. C. Ekiert

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4 papers

Recent·Most cited

Protein-protein interactions in the Mla lipid transport system probed by computational structure prediction and deep mutational scanning

M. R. MacRae, D. Puvanendran, M. A. B. Haase, N. Coudray, L. R. Kolich, C. Lam, M. Baek, G. Bhabha, D. C. Ekiert

The paper maps protein-protein interactions in the Mla lipid transport system using deep mutational scanning and AlphaFold2 structure predictions, revealing overlapping binding sites on MlaC.

bioRxiv · Dec 9, 2022Biophysics

Structure of bacterial phospholipid transporter MlaFEDB with substrate bound

N. Coudray, G. L. Isom, M. R. MacRae, M. N. Saiduddin, G. Bhabha, D. C. Ekiert

The paper reports the cryo-EM structure of the MlaFEDB complex with bound phospholipids, revealing its transport mechanism and substrate binding.

bioRxiv · Jun 2, 2020Biochemistry

Structure of MlaFB uncovers novel mechanisms of ABC transporter regulation

L. R. Kolich, Y.-T. Chang, N. Coudray, S. I. Giacometti, M. R. MacRae, G. L. Isom, E. M. Teran, G. Bhabha, D. C. Ekiert

The paper reports the X-ray structure of MlaFB from E. coli, revealing how the regulatory subunit MlaB stabilizes the nucleotide binding domain and how the C-terminal tail of MlaF mediates dimerization and complex assembly.

bioRxiv · Apr 27, 2020Microbiology

Structure of LetB reveals a tunnel for lipid transport across the bacterial envelope

G. L. Isom, N. Coudray, M. R. MacRae, C. T. McManus, D. C. Ekiert, G. Bhabha

The paper determines the structure of LetB, showing it forms a hydrophobic tunnel for lipid transport across the bacterial envelope.

bioRxiv · Aug 28, 2019Biochemistry