3H50

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

「2ILB」から置き換えられました

3H50 の概要

• エントリーDOI: 10.2210/pdb3h50/pdb
• 分子名称: Tetracenomycin polyketide synthesis protein, ZINC ION, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: tetracenomycin polyketide synthesis protein, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-2, biosynthetic protein
• 由来する生物種: Xanthomonas campestris pv. campestris
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12709.02

構造登録者

Joint Center for Structural Genomics (JCSG) (登録日: 2009-04-21, 公開日: 2009-05-05, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.6 Å)