1itz | pdb_00001itz

Maize Transketolase in complex with TPP

spinqualitylabelsall models 1itz, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1itz is a 3 chain structure with sequence from Maize. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG, TPP Activity: Transketolase, with EC number 2.2.1.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transketolase

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