Karl W. Volz
PhD, University of California, San Diego
Room: 8135 COMRB
Structural Analysis of Cellular Regulatory Proteins
My laboratory analyzes the structural determinants of macromolecular function in a variety of cellular regulatory processes.
Our current research project focuses on the structure and function of iron regulatory protein-1 (IRP1) in its dual roles as a [4Fe-4S] cluster-containing cytosolic aconitase or an mRNA-binding regulatory protein. We elucidated the interconversion mechanism of IRP1 from aconitase to mRNA repressor by solving the first crystal structure of an IRP1:RNA complex.
Previous projects concerned unique non-inhibitory members of the serpin protein superfamily. We solved the structures of the anti-apoptotic viral serpin crmA, the anti-tumor serpin maspin, and the anti-angiogenic factor PEDF to reveal the non-standard functionalities of these important serpin homologues.
Results from our YjgF project presaged the problem of structure-based functional assignment in structural genomics. Our 1.2 Å structure of E. coli YjgF (now known as RidA) was the first for any member of the ubiquitous RidA protein family of deaminases that protect cells from the toxic byproducts of normal metabolism.
Early projects concentrated on CheY, a phosphorylatable protein that regulates bacterial chemotaxis. We determined the structures of apo CheY, activating and inactivating CheY mutants, covalently activated CheY, and CheY in a meta-active state. These functional insights were directly applicable to the hundreds of response regulators in bacterial two-component systems.
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