Imperial College London

ProfessorThomasMeier

Faculty of Natural SciencesDepartment of Life Sciences

Chair in Structural Biology
 
 
 
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Contact

 

+44 (0)20 7594 3056t.meier Website

 
 
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Location

 

501Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Summary

 

SUMMARY

ATP (adenosine triphosphate) is the universal form of energy in living cells to power biochemical reactions such as muscle contraction or brain function. A human being needs approximately his/her own body weight of ATP per day; this large amount is constantly provided by a rotary ATPase, called the ATP synthase. It functions like an energy converter, which uses electric energy at the cell membrane to convert it in chemical energy, ATP. It is very intriguing that the enzyme works like a mechanic machine that has a rotating ion-turbine and a stator in which the ATP can be generated; The ATP synthase is the smallest "nano-machine" known. We are interested in understanding the structure and operation principles of this remarkable machine and to decipher how it works on the molecular level by using the combined power of sophisticated structural biology methods (X-ray crystallography and electron microscopy).

Rotary ATPase recently came also into focus as new drug target against tuberculosis (TB) and a new antibiotic drug, the first anti-TB drug in the last 40 years, blocks rotation of the ATP synthase's ion turbine. We are therefore also interested in understanding the mechanism of action of these drugs to their target from a biochemical and structural point of view and to develop them further. Our research will also help promoting the molecular understanding and development of drugs against dangerous human infection diseases. For more info, see here:  http://principlesofproteinstructure.blogspot.co.uk/2016/08/atp-synthase-new-drug-target-for.html


Research Group



Meier Group June 2018

Meier lab (June 2018). From left to right:

  • Anthony Cheuk, Master student
  • Dr. Michael Hohl, Postdoc, SNF Research Fellow
  • Dr. Yilmaz Alguel, Postdoc
  • Prof. Dr. Thomas Meier, Group leader
  • Dr. Julius Demmer, Postdoc
  • Lisa Uhrig, PhD student
  • Dr. Craig Wilkinson, Postdoc
  • Dr. Mong Sing Lai, Research Technician

Publications

Journals

Dautant A, Meier TK, Hahn A, et al., ATP synthase diseases of mitochondrial genetic origin, Frontiers in Physiology, ISSN:1664-042X

Hahn A, Vonck J, Mills D, et al., 2018, Structure, mechanism, and regulation of the chloroplast ATP synthase, Science, Vol:360, ISSN:0036-8075

Eisel B, Hartrampf FWW, Meier T, et al., 2018, Reversible optical control of F1Fo-ATP synthase using photoswitchable inhibitors, Febs Letters, Vol:592, ISSN:1873-3468, Pages:343-355

Schulz S, Wilkes M, Mills DJ, et al., 2017, Molecular architecture of the N-type ATPase rotor ring from Burkholderia pseudomallei, Embo Reports, Vol:18, ISSN:1469-221X, Pages:526-535

He C, Preiss L, Wang B, et al., 2017, Structural Simplification of Bedaquiline: the Discovery of 3-(4-(N,N-Dimethylaminomethyl)phenyl)quinoline-Derived Antitubercular Lead Compounds, Chemmedchem, Vol:12, ISSN:1860-7179, Pages:106-119

More Publications