9JFB

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

Summary for 9JFB

• Entry DOI: 10.2210/pdb9jfb/pdb
• Descriptor: threonine-phosphate decarboxylase, GLYCEROL, SULFATE ION, ... (6 entities in total)
• Functional Keywords: cobalamin, l-threonine-o-3-phosphate decarboxylase, plp, aminopropanol phosphate, lyase
• Biological source: Rhizobium meliloti (Ensifer meliloti, Sinorhizobium meliloti)
• Total number of polymer chains: 1
• Total formula weight: 37427.81

Authors

Jiang, M.,Guo, S.,Chen, X.,Wei, Q.,Wang, M. (deposition date: 2024-09-04, release date: 2024-10-16)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)