3TKF

1.5 Angstrom Resolution Crystal Structure of K135M Mutant of Transaldolase B (TalA) from Francisella tularensis in Complex with Sedoheptulose 7-phosphate.

Summary for 3TKF

• Entry DOI: 10.2210/pdb3tkf/pdb
• Related: 3IGX 3TE9 3TK7 3TNO 4E0C
• Descriptor: Transaldolase, D-ALTRO-HEPT-2-ULOSE 7-PHOSPHATE, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (6 entities in total)
• Functional Keywords: structural genomics, center for structural genomics of infectious diseases, csgid, alpha-beta barrel/tim barrel, sedoheptulose-7-phosphate:d-glyceraldehyde-3-phosphate glyceronetransferase activity, transferase
• Biological source: Francisella tularensis subsp. tularensis
• Cellular location: Cytoplasm : Q5NFX0
• Total number of polymer chains: 2
• Total formula weight: 79324.66

Authors

Minasov, G.,Light, S.H.,Halavaty, A.,Shuvalova, L.,Papazisi, L.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2011-08-26, release date: 2011-09-07, Last modification date: 2023-09-13)

Primary citation

Light, S.H.,Minasov, G.,Duban, M.E.,Anderson, W.F.
Adherence to Burgi-Dunitz stereochemical principles requires significant structural rearrangements in Schiff-base formation: insights from transaldolase complexes.
Acta Crystallogr.,Sect.D, 70:544-552, 2014

PubMed Abstract: The Bürgi-Dunitz angle (αBD) describes the trajectory of approach of a nucleophile to an electrophile. The adoption of a stereoelectronically favorable αBD 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-à-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.

PubMed: 24531488
DOI: 10.1107/S1399004713030666

Experimental method

X-RAY DIFFRACTION (1.5 Å)