4E0C

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

4E0C の概要

• エントリーDOI: 10.2210/pdb4e0c/pdb
• 関連するPDBエントリー: 3IGX 3TE9 3TK7 3TKF 3TNO 3UPB
• 分子名称: Transaldolase, MAGNESIUM ION, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: structural genomics, niaid, national institute of allergy and infectious diseases, center for structural genomics of infectious diseases, csgid, alpha-beta barrel/tim barrel, transferase
• 由来する生物種: Francisella tularensis subsp. tularensis
• 細胞内の位置: Cytoplasm (By similarity): Q5NFX0
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 77035.50

構造登録者

Light, S.H.,Minasov, G.,Halavaty, A.S.,Shuvalova, L.,Papazisi, L.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (登録日: 2012-03-02, 公開日: 2012-03-14, 最終更新日: 2023-09-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.8 Å)