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Mark Hermodson


 Mark Hermodson


Emeritus Professor of Biochemistry

Department: Biochemistry
Phone: 494.8362

Area of Expertise: Structure and function of membrane transport of proteins

Retired: 2007

Cirriculum Vitae



 Interim Head of Agricultural Research Programs


Dr. Mark Hermodson is responsible for leadership of research programs in agriculture, food and natural resources including fiscal management, and a number of regulatory functions assigned by the Indiana State Legislature. His responsibilities include: program development and overall direction, budget, planning, allocation of resources, support of faculty in the aggressive pursuit of extramural funds, accountability to supporting clientele, and general advocacy for agriculture, food and natural resources research in Indiana . He oversees the research budget, grants and contracts, eight regional Purdue Agricultural Centers, research farms, campus-based research facilities, and a number of research centers. He also coordinates agricultural research with the College of Consumer and Family Sciences and School of Veterinary Medicine, and assures effective linkage with other campus research communities and Cooperative Extension.






The high affinity membrane transport system for ribose in Escherichia coli is a member of a large family of membrane transporters found in all forms of living organisms. Homologous systems in humans include the cystic fibrosis related transmembrane conductance regulator (CFTR), multiple drug resistance (MDR) proteins, and the TAP proteins which load foreign antigens onto MHC Class I antigen-presenting molecules. Membrane transporters of this family have at least one, usually two, ATP-binding domains of about 250 amino acids having quite hydrophilic character. These ATP-binding cassettes (ABC) are clearly homologous from bacteria to humans, implying a common protein tertiary structure and similarity of mechanisms. They are associated with extremely hydrophobic domains of 250 to 300 amino acids, either as parts of the same protein or as separate subunits of a multimeric complex. The CFTR and MDR proteins each have two ABC's and two hydrophobic domains, producing proteins of 1300 to 1500 amino acids. In contrast, the ribose transporter of E. coli has an ATP-binding protein, RbsA, which has only two ABC's in a 501 amino acid protein (thus creating a protein with homologous N- and C-terminal halves). The hydrophobic part of the transporter, RbsC, is encoded on a separate gene. This simplifies production and purification of the constituents of the transporter.

We have produced and purified RbsA and RbsC in milligram quantities for structural analyses. We have also produced the N-terminal half molecule of RbsA, which constitutes a single ABC, and that molecule has produced large crystals. The structure has been determined by X-ray diffraction analysis, the first structure of an ABC from any member of this family to be solved. We are screening conditions for crystallizing the whole RbsA molecule and also RbsC. No suitable crystals for X-ray analysis have been obtained yet.

We have successfully reconstituted the transport system in lipid vesicles using the purified RbsA and RbsC and have trapped the whole transport complex using vanadate to inhibit the ATPase activity at the transition state. Mechanistic studies are being performed using these systems, and we are attempting to grow crystals of the whole complex.

In a related study, the repressor that regulates expression of the ribose transport system, RbsR, has been purified and crystallized in complex with an 18 base pair operator DNA fragment. The X-ray structure of this complex has been determined and will be compared to the structures of PurR and LacI, homologous repressor proteins. Dr. Howard Zalkin, of this department, and Dr. Richard Brennan, Oregon State University, solved the structure of holo-PurR (with hypoxanthine bound) in complex with its operator DNA and also apo-PurR corepressor-binding domain (lacking the DNA-binding domain). The structure of RbsR will be informative, since the apo-form of RbsR binds DNA most strongly, the opposite mechanism from PurR. Thus, comparison of the two structures will allow us to deduce the features which contribute to stabilizing the binding to the DNA.




Stewart, J.B. and Hermodson, M.A. Topology of RbsC, the membrane component of the Escherichia coli ribose transporter. J of Bact 185: 5234-5239 (2003).


Zaitseva, J., Zhang, H., and Hermodson, M. A. The proteins encoded by the rbs operon of E. coli: II. Use of chimeric protein constructs to isolate and characterize RbsC. Protein Science 5:1100-1107 (1996).


Barroga, C. F., Zhang, H., Wajih, N., Bouyer, J. H., and Hermodson, M. A. The proteins encoded by the rbs operon of E. coli: I. Overproduction, purification, characterization and functional analysis of RbsA. Protein Science 5:1093-1099 (1996).


Björkman, A. J., Binnie, R. A., Cole, L. B., Zhang, H., Hermodson, M. A., and Mowbray, S. L. Identical mutations at corresponding positions in two homologous proteins with non-identical effects. J. Biol. Chem 269:11196-11200 (1994).


Binnie, R. A., Zhang, H., Mowbray, S., and Hermodson, M. A. Functional mapping of the surface of Escherichia coli ribose-binding protein: Mutations that affect chemotaxis and transport. Protein Science 1:1642-1651 (1992).


Mauzy, C. A., and Hermodson, M. A. Structural homology between rbs repressor and ribose binding protein implies functional similarity. Protein Science 1:843-849 (1992).