4e0c | pdb_00004e0c

1.8 Angstrom Resolution Crystal Structure of Transaldolase from Francisella tularensis (phosphate-free)

spinqualitylabelsall models 4e0c, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4e0c is a 2 chain structure with sequence from Fratt. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, MG Related: 3igx, 3tk7, 3tno, 3upb, 3te9, 3tkf Gene: FTT_1093c, talA (FRATT) Activity: Transaldolase, with EC number 2.2.1.2 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed The Burgi-Dunitz angle (alphaBD) describes the trajectory of approach of a nucleophile to an electrophile. The adoption of a stereoelectronically favorable alphaBD can necessitate significant reactive-group repositioning over the course of bond formation. In the context of enzyme catalysis, interactions with the protein constrain substrate rotation, which could necessitate structural transformations during bond formation. To probe this theoretical framework vis-a-vis biocatalysis, Schiff-base formation was analysed in Francisella tularensis transaldolase (TAL). Crystal structures of wild-type and Lys-->Met mutant TAL in covalent and noncovalent complexes with fructose 6-phosphate and sedoheptulose 7-phosphate clarify the mechanism of catalysis and reveal that substrate keto moieties undergo significant conformational changes during Schiff-base formation. Structural changes compelled by the trajectory considerations discussed here bear relevance to bond formation in a variety of constrained enzymic/engineered systems and can inform the design of covalent therapeutics. Adherence to Burgi-Dunitz stereochemical principles requires significant structural rearrangements in Schiff-base formation: insights from transaldolase complexes.,Light SH, Minasov G, Duban ME, Anderson WF Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):544-52. doi:, 10.1107/S1399004713030666. Epub 2014 Jan 31. PMID:24531488 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA