9JFB

Crystal structure of L-threonine-O-3-phosphate decarboxylase CobC

9JFB の概要

• エントリーDOI: 10.2210/pdb9jfb/pdb
• 分子名称: threonine-phosphate decarboxylase, GLYCEROL, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: cobalamin, l-threonine-o-3-phosphate decarboxylase, plp, aminopropanol phosphate, lyase
• 由来する生物種: Rhizobium meliloti (Ensifer meliloti, Sinorhizobium meliloti)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37427.81

構造登録者

Jiang, M.,Guo, S.,Chen, X.,Wei, Q.,Wang, M. (登録日: 2024-09-04, 公開日: 2024-10-16)

主引用文献

Jiang, M.,Guo, S.,Chen, X.,Wei, Q.,Wang, M.
Crystal structure of l-threonine-O-3-phosphate decarboxylase CobC from Sinorhizobium meliloti involved in vitamin B 12 biosynthesis.
Biochem.Biophys.Res.Commun., 734:150767-150767, 2024

PubMed Abstract: Vitamin B is involved in many important biochemical reactions for humans, and its deficiency can lead to serious diseases. The industrial production of vitamin B is achieved through microbial fermentation. In this work, we determine the crystal structures of the l-threonine-O-3-phosphate (Thr-P) decarboxylase CobC from Sinorhizobium meliloti (SmCobC), an industrial vitamin B-producing bacterium, in apo form and in complex with a reaction intermediate. Our structures supported the Thr-P decarboxylase activity of SmCobC and revealed that the positively charged substrate-binding pocket between the large and small domains determines its substrate selectivity for Thr-P. Moreover, our results provided evidence for the proposition that the AP-P linker is formed by direct incorporation of AP-P in the biosynthetic pathway of vitamin B in S.meliloti.

PubMed: 39366178
DOI: 10.1016/j.bbrc.2024.150767

実験手法

X-RAY DIFFRACTION (2.2 Å)