Structural highlights
3te9 is a 2 chain structure with sequence from "francisella_tularensis_subsp._nearctica"_olsufjev_1970 "francisella tularensis subsp. nearctica" olsufjev 1970. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , , |
| Related: | 3igx, 4e0c, 3tk7, 3tno, 3tkf |
| Gene: | FTT_1093c, talA ("Francisella tularensis subsp. nearctica" Olsufjev 1970) |
| Activity: | Transaldolase, with EC number 2.2.1.2 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[Q5NFX0_FRATT] Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway (By similarity).[RuleBase:RU004155][SAAS:SAAS004730_004_006516]
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Light SH, Minasov G, Duban ME, Anderson WF. Adherence to Burgi-Dunitz stereochemical principles requires significant structural rearrangements in Schiff-base formation: insights from transaldolase complexes. Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):544-52. doi:, 10.1107/S1399004713030666. Epub 2014 Jan 31. PMID:24531488 doi:http://dx.doi.org/10.1107/S1399004713030666
