LUO MIN

LUO MIN

LUO MIN

Assistant Professor

Department of Biological Sciences,
National University of Singapore,
14 Science Drive 4, Singapore 117543

66012310
dbslmin@nus.edu.sg


Academic Qualifications

Postdoc. (Harvard Medical School, USA), D. Phil. (U. of Missouri-Columbia, USA), B. Sc. (Shandong U., China)

Major Research Interests

Across-membrane translocation plays a fundamental role in all living cells. Our lab aims to dissect the molecular mechanism of membrane machineries using a structural biology approach that combines cryo-EM (Fig. 1) with techniques from membrane reconstitution, biochemistry, molecular biology, biophysics and cell biology.  We focus on the study of challenging transmembrane proteins such as ABC transporters that play essential role in human health and disease. We also develop and apply novel approaches for identification of new membrane protein complexes in mitochondria.

 

Figure 1

 

Figure 2

 

Currently, our primary interest is to combine biochemical and biophysical techniques to address fundamental questions in important drug targets of membrane proteins in mitochondria (Fig. 2), specifically on their regulation in 1) iron/ROS homeostasis, and 2) mitochondrial morphology.

Selected publications

  1. Luo M#, Zhou WC.#(co-first), Patel H, Srivastava AP, Symersky J, Bonar MM, Faraldo-Gómez JD, Liao MF., Mueller DM. Bedaquiline inhibits the yeast and human mitochondrial ATP synthases.  Commun. Biol. 2020, 19;3(1):452.

  2. Xiao YB.#, Luo M.# (co-first), Dolan E. A., Liao MF., Ke AL.. Structure Basis for RNA-guided DNA degradation by Cascade and Cas3. Science. (2018) doi: 10.1126/science.aat0839

  3. Srivastava A.#, Luo M.# (co-first), Zhou WC., Symersky J., Bai DY., Chambers G. M., Faraldo-Gómez JD, Liao MF., Mueller DM. High-resolution cryo-EM analysis of the yeast ATP synthase in a lipid membrane. Science. (2018) doi: 10.1126/science.aas9699.

  4. Xiao YB.#, Luo M.# (co-first), Hayes P.R., Kim J., Ng S., Ding F., Liao MF., Ke AL.. Structure Basis for Directional R-loop Formation and Substrate Handover Mechanisms in Type I CRISPR-Cas System. Cell.  (2017) 170(1):48-60.e11.

  5. Luo M, T.T. Gamage, B.W. Arentson, K.N. Schlasner, D.F. Becker and J.J. Tanner. Structures of Proline Utilization A Reveal the Fold and Functions of the Aldehyde Dehydrogenase Superfamily Domain of Unknown Function. J Biol Chem. (2016) 291(46):24065-24075.

  6. Luo M, Tanner JJ. Structural Basis of Substrate Recognition by Aldehyde Dehydrogenase 7A1. Biochemistry (2015) 8;54(35):5513-22.

  7. Luo M, KS Gates, MT Henzl, and JJ Tanner. Diethylaminobenzaldehyde is a Covalent, Irreversible Inactivator of ALDH7A1.

  8. ACS Chem. Biol. (2015) 10(3):693-697

  9. Luo M, Christgen, S., Sanyal, N, Arentson BW, Becker DF, Tanner JJ. Evidence that the C-terminal Domain of a Type B PutA Protein Contributes to Aldehyde Dehydrogenase Activity and Substrate Channeling. Biochemistry (2014) 53(35):5661-73.

  10. Luo M, R.K. Singh, and Tanner JJ. Structural Determinants of Oligomerization of 1-Pyrroline-5-Carboxylate Dehydrogenase: Identification of a Hexamerization Hot Spot. J. Mol. Biol. (2013) 425(17):3106-3120.

  11. Luo M, Arentson BW, Srivastava D, Becker DF, and Tanner JJ. Crystal Structures and Kinetics of Monofunctional Proline Dehydrogenase Provide Insight into substrate Recognition and Conformational Changes Associated With Flavin Reduction and Product release. Biochemistry (2012) 51(50):10099-108) .