Open AccessConformational changes associated with the binding of zinc acetate at the putative active site of Xc TcmJ, a cupin from Xanthomonas campestris pv. campestris
Author(s) -
Axelrod Herbert L.,
Kozbial Piotr,
McMullan Daniel,
Krishna S. Sri,
Miller Mitchell D.,
Abdubek Polat,
Acosta Claire,
Astakhova Tamara,
Carlton Dennis,
Caruthers Jonathan,
Chiu HsiuJu,
Clayton Thomas,
Deller Marc C.,
Duan Lian,
Elias Ylva,
Feuerhelm Julie,
Grzechnik Slawomir K.,
Grant Joanna C.,
Han Gye Won,
Jaroszewski Lukasz,
Jin Kevin K.,
Klock Heath E.,
Knuth Mark W.,
Kumar Abhinav,
Marciano David,
Morse Andrew T.,
Murphy Kevin D.,
Nigoghossian Edward,
Okach Linda,
Oommachen Silvya,
Paulsen Jessica,
Reyes Ron,
Rife Christopher L.,
Tien Henry J.,
Trout Christina V.,
Van Den Bedem Henry,
Weekes Dana,
White Aprilfawn,
Xu Qingping,
Zubieta Chloe,
Hodgson Keith O.,
Wooley John,
Elsliger MarcAndré,
Deacon Ashley M.,
Godzik Adam,
Lesley Scott A.,
Wilson Ian A.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109021988
Subject(s) - xanthomonas campestris , zinc , chemistry , microbiology and biotechnology , stereochemistry , biology , biochemistry , gene , organic chemistry
In the plant pathogen Xanthomonas campestris pv. campestris , the product of the tcmJ gene, Xc TcmJ, encodes a protein belonging to the RmlC family of cupins. Xc TcmJ was crystallized in a monoclinic space group ( C 2) 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 Xc TcmJ 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 Xc TcmJ. 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.