October 9 - 12, 2012
Building 10 & Natcher Conference Center
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- Opening Plenary Session
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Towards a structure of the fungal outer mitochondrial membrane protein Mdm10
| Friday, November 08, 2013 — Poster Session IV | |||
|---|---|---|---|
2:00 p.m. – 4:00 p.m. |
FAES Academic Center (Upper-Level Terrace) |
NIDDK |
STRUCTBIO-15 |
Authors
- A.M. Stanley
- S.K. Buchanan
Abstract
Recent years have seen a significant increase in the occurrence of systemic fungal infections, and fungi are among the leading causes of hospital-acquired bloodstream infections. As fungi are eukaryotic, it is challenging to identify pharmacological targets that can be exploited to impair fungal viability without compromising the host. Conserved only in fungi, Mdm10 is an integral membrane β-barrel protein with an important dual role in mitochondrial biology, functioning both in the biogenesis of outer mitochondrial membrane (OMM) proteins and mitochondrial morphology. We are using structural and biochemical approaches to characterize the Mdm10 protein. Strategies for the expression and purification of Mdm10 homologs in quantities sufficient for crystallography experiments will be discussed. Both in vivo heterologous overexpression of natively folded protein and in vitro refolding approaches are being tried. Work is also underway to examine the effects of mutations and truncations on Mdm10 function. These experiments will address the interaction of Mdm10 with its binding partners and be used to identify improved constructs for crystallography. High-resolution structural information, in combination with functional data, will provide valuable insight into the function of Mdm10 and suggest ways to exploit the protein as a target for novel anti-fungal therapeutics.
