2x2g

CRYSTALLOGRAPHIC BINDING STUDIES WITH AN ENGINEERED MONOMERIC VARIANT OF TRIOSEPHOSPHATE ISOMERASE

spinqualitylabelsall models 2x2g, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2x2g is a 2 chain structure. This structure supersedes the now removed PDB entry 2x0m. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 3PG Related: 2v2c, 1kv5, 1iih, 6tim, 2wsr, 3tim, 2x16, 1iig, 2v2h, 1dkw, 2vem, 1ttj, 2x1s, 2v5l, 4tim, 2vei, 2x1t, 5tim, 2x1r, 1tsi, 1mss, 2wsq, 2j27, 1tpf, 1tpe, 1tpd, 2vel, 2vek, 2v0t, 1trd, 1tri, 1ml1, 2j24, 2x1u, 1ag1, 2ven, 1mtm, 2v2d, 1tti Activity: Triose-phosphate isomerase, with EC number 5.3.1.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 Crystallographic binding studies have been carried out to probe the active-site binding properties of a monomeric variant (A-TIM) of triosephosphate isomerase (TIM). These binding studies are part of a structure-based directed-evolution project aimed towards changing the substrate specificity of monomeric TIM and are therefore aimed at finding binders which are substrate-like molecules. A-TIM has a modified more extended binding pocket between loop-7 and loop-8 compared with wild-type TIM. The A-TIM crystals were grown in the presence of citrate, which is bound in the active site of each of the two molecules in the asymmetric unit. In this complex, the active-site loops loop-6 and loop-7 adopt the closed conformation, similar to that observed in liganded wild-type TIM. Extensive crystal-soaking protocols have been developed to flush the bound citrate out of the active-site pocket of both molecules and the crystal structure shows that the unliganded open conformation of the A-TIM active site is the same as in unliganded wild-type TIM. It is also shown that sulfonate compounds corresponding to the transition-state analogue 2-phosphoglycolate bind in the active site, which has a closed conformation. It is also shown that the new binding pocket of A-TIM can bind 3-phosphoglycerate (3PGA; an analogue of a C4-sugar phosphate) and 4-phospho-D-erythronohydroxamic acid (4PEH; an analogue of a C5-sugar phosphate). Therefore, these studies have provided a rationale for starting directed-evolution experiments aimed at generating the catalytic properties of a C5-sugar phosphate isomerase on the A-TIM framework. Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase.,Salin M, Kapetaniou EG, Vaismaa M, Lajunen M, Casteleijn MG, Neubauer P, Salmon L, Wierenga RK Acta Crystallogr D Biol Crystallogr. 2010 Aug;66(Pt 8):934-44. Epub 2010, Jul 14. PMID:20693693 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Triose phosphate isomerase 3D structures

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