2PE7

Thaumatin from Thaumatococcus Danielli in complex with tris-dipicolinate Europium

Summary for 2PE7

• Entry DOI: 10.2210/pdb2pe7/pdb
• Descriptor: Preprothaumatin I, EUROPIUM ION, L(+)-TARTARIC ACID, ... (5 entities in total)
• Functional Keywords: thaumatin, tris-dipicolinate europium, plant protein
• Biological source: Thaumatococcus daniellii (Katemfe)
• Total number of polymer chains: 1
• Total formula weight: 23181.54

Authors

Pompidor, G.,Vicat, J.,Kahn, R. (deposition date: 2007-04-02, release date: 2008-04-22, Last modification date: 2024-10-30)

Primary citation

Pompidor, G.,Maury, O.,Vicat, J.,Kahn, R.
A dipicolinate lanthanide complex for solving protein structures using anomalous diffraction.
Acta Crystallogr.,Sect.D, 66:762-769, 2010

PubMed Abstract: Tris-dipicolinate lanthanide complexes were used to prepare derivative crystals of six proteins: hen egg-white lysozyme, turkey egg-white lysozyme, thaumatin from Thaumatococcus daniellii, urate oxidase from Aspergillus flavus, porcine pancreatic elastase and xylanase from Trichoderma reesei. Diffraction data were collected using either synchrotron radiation or X-rays from a laboratory source. In all cases, the complex turned out to be bound to the protein and the phases determined using the anomalous scattering of the lanthanide led to high-quality electron-density maps. The binding mode of the complex was characterized from the refined structures. The lanthanide tris-dipicolinate was found to bind through interactions between carboxylate groups of the dipicolinate ligands and hydrogen-bond donor groups of the protein. In each binding site, one enantiomeric form of the complex is selected from the racemic solution according to the specific site topology. For hen egg-white lysozyme and xylanase, derivative crystals obtained by cocrystallization belonged to a new monoclinic C2 crystal form that diffracted to high resolution.

PubMed: 20606256
DOI: 10.1107/S0907444910010954

Experimental method

X-RAY DIFFRACTION (1.46 Å)