Open and closed conformations of two SpoIIAA-like proteins (YP_749275.1 and YP_001095227.1) provide insights into membrane association and ligand binding
Year: 2009
Type: article
Abstract: The crystal structures of the proteins encoded by the YP_749275.1 and YP_001095227.1 genes from Shewanella frigidimarina and S. loihica, respectively, have been determined at 1.8 and 2.25 Å resolution, respectively. These proteins are members of a novel family of bacterial proteins that adopt the α/β SpoIIAA-like fold found in STAS and CRAL-TRIO domains. Despite sharing 54% sequence identity, these two proteins adopt distinct conformations arising from different dispositions of their α2 and α3 helices. In the `open' conformation (YP_001095227.1), these helices are 15 Å apart, leading to the creation of a deep nonpolar cavity. In the `closed' structure (YP_749275.1), the helices partially unfold and rearrange, occluding the cavity and decreasing the solvent-exposed hydrophobic surface. These two complementary structures are reminiscent of the conformational switch in CRAL-TRIO carriers of hydrophobic compounds. It is suggested that both proteins may associate with the lipid bilayer in their `open' monomeric state by inserting their amphiphilic helices, α2 and α3, into the lipid bilayer. These bacterial proteins may function as carriers of nonpolar substances or as interfacially activated enzymes.
Authors: Abhinav Kumar, Andrei Lomize, Kevin K. Jin, Dennis Carlton, Mitchell D. Miller, Lukasz Jaroszewski, Polat Abdubek, Tamara Astakhova, Herbert L. Axelrod, Hsiu-Ju Chiu, Thomas Clayton, Debanu Das, Marc C. Deller, Lian Duan, Julie Feuerhelm, Joanna C. Grant, Anna Grzechnik, Gye Won Han, Heath E. Klock, Mark W. Knuth, Piotr Kozbial, S. Sri Krishna, David Marciano, Daniel McMullan, Andrew T. Morse, Edward Nigoghossian, Linda Okach, Ron Reyes, Christopher L. Rife, Natasha Sefcovic, Henry J. Tien, Christine B. Trame, Henry van den Bedem, Dana Weekes, Qingping Xu, Keith O. Hodgson, John Wooley, Marc-André Elsliger, Ashley M. Deacon, Adam Godzik, Scott A. Lesley, Ian A. Wilson
Institutions: SLAC National Accelerator Laboratory, Joint Center for Structural Genomics, Stanford Synchrotron Radiation Lightsource, University of Michigan, Scripps Research Institute, Sanford Burnham Prebys Medical Discovery Institute, University of California San Diego, Genomics Institute of the Novartis Research Foundation
Language: English
Subfield: Materials Chemistry
Field: Materials Science
Domain: Physical Sciences
Open Access status: hybrid
OpenAlex ID: W1994888409