3r5e | pdb_00003r5e

TRANSALDOLASE from Corynebacterium glutamicum

spinqualitylabelsall models 3r5e, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3r5e is a 1 chain structure with sequence from "micrococcus_glutamicus"_kinoshita_et_al._1958 "micrococcus glutamicus" kinoshita et al. 1958. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 Related: 3r8r Gene: cg1776, Cgl1575, tal ("Micrococcus glutamicus" Kinoshita et al. 1958) Activity: Transaldolase, with EC number 2.2.1.2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [Q8NQ64_CORGL] Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway (By similarity).[HAMAP-Rule:MF_00493] Publication Abstract from PubMed Transaldolase (Tal) is involved in the central carbon metabolism, i.e. the non-oxidative pentose phosphate pathway, and is therefore a ubiquitous enzyme. However, Tals show a low degree in sequence identity and vary in length within the enzyme family which previously led to the definition of five subfamilies. We wondered how this variation is conserved in structure and function. To answer this question we characterised and compared the Tals from Bacillus subtilis, Corynebacterium glutamicum and Escherichia coli, each belonging to a different subfamily, with respect to their biochemical properties and structures. The overall structure of the Tal domain, a (beta/alpha)(8) -barrel fold, is well conserved between the different subfamilies but the enzymes show different degrees of oligomerisation (monomer, dimer and decamer). The substrate specificity of the three enzymes investigated is quite similar which is reflected in the conservation of the active site, the phosphate binding site as well as the position of a catalytically important water molecule. All decameric enzymes characterised so far appear to be heat stable no matter whether they originate from a mesophilic or thermophilic organism. Hence, the thermostability might be due to the structural properties, i.e. tight packing, of these enzymes. Database The crystal structures have been deposited in the Protein Data Bank with accession code 3R8R for BsTal and 3R5E for CgTal. Structured digital abstract * BsTal and BsTal bind by x-ray crystallography (View interaction) * BsTal and BsTal bind by x-ray crystallography (View interaction). Conservation of structure and mechanism within the transaldolase enzyme family.,Samland AK, Baier S, Schurmann M, Inoue T, Huf S, Schneider G, Sprenger GA, Sandalova T FEBS J. 2011 Dec 25. doi: 10.1111/j.1742-4658.2011.08467.x. PMID:22212631 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transaldolase

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