Imperial College London
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DrMichaelHohl

Faculty of Medicine, Department of Infectious Disease

Research Associate
 
 
 
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Contact

 

m.hohl Website

 
 
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Location

 

Sir Alexander Fleming BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Bukowska:2015:10.1021/acs.biochem.5b00188,
author = {Bukowska, MA and Hohl, M and Geertsma, ER and Hürlimann, LM and Grütter, MG and Seeger, MA},
doi = {10.1021/acs.biochem.5b00188},
journal = {Biochemistry},
pages = {3086--3099},
title = {A Transporter Motor Taken Apart: Flexibility in the Nucleotide Binding Domains of a Heterodimeric ABC Exporter.},
url = {http://dx.doi.org/10.1021/acs.biochem.5b00188},
volume = {54},
year = {2015}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - ABC exporters are ubiquitous multidomain transport proteins that couple ATP hydrolysis at a pair of nucleotide binding domains to substrate transport across the lipid bilayer mediated by two transmembrane domains. Recently, the crystal structure of the heterodimeric ABC exporter TM287/288 was determined. One of its asymmetric ATP binding sites is called the degenerate site; it binds nucleotides tightly but is impaired in terms of ATP hydrolysis. Here we report the crystal structures of both isolated motor domains of TM287/288. Unexpectedly, structural elements constituting the degenerate ATP binding site are disordered in these crystals and become structured only in the context of the full-length transporter. In addition, hydrogen bonding patterns of key residues, including those of the catalytically important Walker B and the switch loop motifs, are fundamentally different in the solitary NBDs compared to those in the intact transport protein. The structures reveal crucial interdomain contacts that need to be established for the proper assembly of the functional transporter complex.
AU  - Bukowska,MA
AU  - Hohl,M
AU  - Geertsma,ER
AU  - Hürlimann,LM
AU  - Grütter,MG
AU  - Seeger,MA
DO  - 10.1021/acs.biochem.5b00188
EP  - 3099
PY  - 2015///
SP  - 3086
TI  - A Transporter Motor Taken Apart: Flexibility in the Nucleotide Binding Domains of a Heterodimeric ABC Exporter.
T2  - Biochemistry
UR  - http://dx.doi.org/10.1021/acs.biochem.5b00188
UR  - https://www.ncbi.nlm.nih.gov/pubmed/25947941
VL  - 54
ER  -
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