Conformational changes associated with the binding of zinc acetate at the putative active site ofXcTcmJ, a cupin fromXanthomonas campestrispv.campestris
Year: 2009
Type: article
Abstract: In the plant pathogen Xanthomonas campestris pv. campestris, the product of the tcmJ gene, XcTcmJ, encodes a protein belonging to the RmlC family of cupins. XcTcmJ was crystallized in a monoclinic space group (C2) in the presence of zinc acetate and the structure was determined to 1.6 Å resolution. Previously, the apo structure has been reported in the absence of any bound metal ion [Chin et al. (2006), Proteins, 65, 1046-1050]. The most significant difference between the apo structure and the structure of XcTcmJ described here is a reorganization of the binding site for zinc acetate, which was most likely acquired from the crystallization solution. This site is located in the conserved metal ion-binding domain at the putative active site of XcTcmJ. In addition, an acetate was also bound within coordination distance of the zinc. In order to accommodate this binding, rearrangement of a conserved histidine ligand is required as well as several nearby residues within and around the putative active site. These observations indicate that binding of zinc serves a functional role in this cupin protein.
Authors: Herbert L. Axelrod, Piotr Kozbial, Daniel McMullan, S. Sri Krishna, Mitchell D. Miller, Polat Abdubek, Claire Acosta, Tamara Astakhova, Dennis Carlton, Jonathan Caruthers, Hsiu-Ju Chiu, Thomas Clayton, Marc C. Deller, Lian Duan, Ylva Elias, Julie Feuerhelm, Slawomir K. Grzechnik, Joanna C. Grant, Gye Won Han, Lukasz Jaroszewski, Kevin K. Jin, Heath E. Klock, Mark W. Knuth, Abhinav Kumar, David Marciano, Andrew T. Morse, Kevin D. Murphy, Edward Nigoghossian, Linda Okach, Silvya Oommachen, Jessica Paulsen, Ron Reyes, Christopher L. Rife, Henry J. Tien, Christina V. Trout, Henry van den Bedem, Dana Weekes, Aprilfawn White, Qingping Xu, Chloe Zubieta, 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, Sanford Burnham Prebys Medical Discovery Institute, Genomics Institute of the Novartis Research Foundation, University of California San Diego, Scripps Research Institute
Language: English
Subfield: Materials Chemistry
Field: Materials Science
Domain: Physical Sciences
Open Access status: hybrid
OpenAlex ID: W2070199868