Journal article

A suite of Switch I and Switch II mutant structures from the G-protein domain of FeoB

Miriam-Rose Ash, Megan J Maher, J Mitchell Guss, Mika Jormakka

Acta Crystallographica Section D, Structural Biology | WILEY-BLACKWELL | Published : 2011

Abstract

The acquisition of ferrous iron in prokaryotes is achieved by the G-protein-coupled membrane protein FeoB. This protein possesses a large C-terminal membrane-spanning domain preceded by two soluble cytoplasmic domains that are together termed 'NFeoB'. The first of these soluble domains is a GTPase domain (G-domain), which is then followed by an entirely α-helical domain. GTP hydrolysis by the G-domain is essential for iron uptake by FeoB, and various NFeoB mutant proteins from Streptococcus thermophilus have been constructed. These mutations investigate the role of conserved amino acids from the protein's critical Switch regions. Five crystal structures of these mutant proteins have been det..

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University of Melbourne Researchers

Grants

Awarded by National Health and Medical Research Council


Funding Acknowledgements

This study was supported by the National Health and Medical Research Council (grant Nos. 570784 and 632703). This research was undertaken on the MX1 and MX2 beamlines at the Australian Synchrotron, Victoria, Australia. MJM is a Cancer Institute of NSW Career Development Fellow. M-RA is the recipient of an Australian Postgraduate Award.