This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1itz
From Proteopedia
|
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 and 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 Thu Feb 21 13:15:37 2008
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
