1itz
From Proteopedia
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Maize Transketolase in complex with TPP
Overview
The gene specifying plastid transketolase (TK) of maize (Zea mays) was, cloned from a cDNA library by southern blotting using a heterologous probe, from sorghum (Sorghum bicolor). A recombinant fusion protein comprising, thioredoxin of Escherichia coli and mature TK of maize was expressed at a, high level in E. coli and cleaved with thrombin, affording plastid TK. The, protein in complex with thiamine pyrophoshate was crystallized, and its, structure was solved by molecular replacement. The enzyme is a C2, symmetric homodimer closely similar to the enzyme from yeast, (Saccharomyces cerevisiae). Each subunit is folded into three domains. The, two topologically equivalent active sites are located in the subunit, interface region and resemble those of the yeast enzyme.
About this Structure
1ITZ is a Single protein structure of sequence from Zea mays with MG and TPP as ligands. Active as Transketolase, with EC number 2.2.1.1 Full crystallographic information is available from OCA.
Reference
Structure and properties of an engineered transketolase from maize., Gerhardt S, Echt S, Busch M, Freigang J, Auerbach G, Bader G, Martin WF, Bacher A, Huber R, Fischer M, Plant Physiol. 2003 Aug;132(4):1941-9. PMID:12913150
Page seeded by OCA on Tue Nov 20 17:39:46 2007
Categories: Single protein | Transketolase | Zea mays | Bacher, A. | Bader, G. | Busch, M. | Echt, S. | Fischer, M. | Freigang, J. | Gerhardt, S. | Huber, R. | MG | TPP | Calvin cycle | Cofactor | Plant | Thiamine pyrophosphate
