3UPB

1.5 Angstrom Resolution Crystal Structure of Transaldolase from Francisella tularensis in Covalent Complex with Arabinose-5-Phosphate

3UPB の概要

• エントリーDOI: 10.2210/pdb3upb/pdb
• 関連するPDBエントリー: 3IGX 3TE9 3TK7 3TKF 3TNO
• 分子名称: Transaldolase, HEXAETHYLENE GLYCOL, ARABINOSE-5-PHOSPHATE, ... (6 entities in total)
• 機能のキーワード: structural genomics, 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 : Q5NFX0
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 78211.32

構造登録者

Light, S.H.,Minasov, G.,Shuvalova, L.,Papazisi, L.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (登録日: 2011-11-17, 公開日: 2011-11-30, 最終更新日: 2024-11-06)

主引用文献

Light, S.H.,Anderson, W.F.
Arabinose 5-phosphate covalently inhibits transaldolase.
J.Struct.Funct.Genom., 15:41-44, 2014

PubMed Abstract: Arabinose 5-phosphate (A5P) is the aldopentose version of the ketohexose fructose 6-phosphate (F6P), having identical stereochemistry but lacking atoms corresponding to the 1-carbon and 1-hydroxyl. Despite structural similarity and conservation of the reactive portion of F6P, F6P acts as a substrate whereas A5P is reported to be an inhibitor of transaldolase. To address the lack of A5P reactivity we determined a crystal structure of the Francisella tularensis transaldolase in complex with A5P. This structure reveals that like F6P, A5P forms a covalent Schiff base with active site Lys135. Unlike F6P, A5P binding fails to displace an ordered active site water molecule. Retaining this water necessitates conformational changes at the A5P-protein linkage that possibly hinder reactivity. The findings presented here show the basis of A5P inhibition and suggest an unusual mechanism of competitive, reversible-covalent transaldolase regulation.

PubMed: 24510200
DOI: 10.1007/s10969-014-9174-1

実験手法

X-RAY DIFFRACTION (1.5 Å)