3H50

CRYSTAL STRUCTURE OF A TETRACENOMYCIN POLYKETIDE SYNTHESIS PROTEIN (TCMJ) FROM XANTHOMONAS CAMPESTRIS PV. CAMPESTRIS AT 1.60 A RESOLUTION

Replaces:  2ILB

Summary for 3H50

• Entry DOI: 10.2210/pdb3h50/pdb
• Descriptor: Tetracenomycin polyketide synthesis protein, ZINC ION, ACETATE ION, ... (4 entities in total)
• Functional Keywords: tetracenomycin polyketide synthesis protein, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-2, biosynthetic protein
• Biological source: Xanthomonas campestris pv. campestris
• Total number of polymer chains: 1
• Total formula weight: 12709.02

Authors

Joint Center for Structural Genomics (JCSG) (deposition date: 2009-04-21, release date: 2009-05-05, Last modification date: 2024-10-30)

Primary citation

Axelrod, H.L.,Kozbial, P.,McMullan, D.,Krishna, S.S.,Miller, M.D.,Abdubek, P.,Acosta, C.,Astakhova, T.,Carlton, D.,Caruthers, J.,Chiu, H.J.,Clayton, T.,Deller, M.C.,Duan, L.,Elias, Y.,Feuerhelm, J.,Grzechnik, S.K.,Grant, J.C.,Han, G.W.,Jaroszewski, L.,Jin, K.K.,Klock, H.E.,Knuth, M.W.,Kumar, A.,Marciano, D.,Morse, A.T.,Murphy, K.D.,Nigoghossian, E.,Okach, L.,Oommachen, S.,Paulsen, J.,Reyes, R.,Rife, C.L.,Tien, H.J.,Trout, C.V.,van den Bedem, H.,Weekes, D.,White, A.,Xu, Q.,Zubieta, C.,Hodgson, K.O.,Wooley, J.,Elsliger, M.A.,Deacon, A.M.,Godzik, A.,Lesley, S.A.,Wilson, I.A.
Conformational changes associated with the binding of zinc acetate at the putative active site of XcTcmJ, a cupin from Xanthomonas campestris pv. campestris.
Acta Crystallogr.,Sect.F, 66:1347-1353, 2010

PubMed 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.

PubMed: 20944231
DOI: 10.1107/S1744309109021988

Experimental method

X-RAY DIFFRACTION (1.6 Å)