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Crystal structure of L-threonine-O-3-phosphate decarboxylase CobCCrystal structure of L-threonine-O-3-phosphate decarboxylase CobC
Structural highlights
FunctionA0A499W357_RHIML Decarboxylates L-threonine-O-3-phosphate to yield (R)-1-amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.[ARBA:ARBA00003444] Publication Abstract from PubMedVitamin B(12) is involved in many important biochemical reactions for humans, and its deficiency can lead to serious diseases. The industrial production of vitamin B(12) 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(12)-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(12) in S.meliloti. Crystal structure of l-threonine-O-3-phosphate decarboxylase CobC from Sinorhizobium meliloti involved in vitamin B(12) biosynthesis.,Jiang M, Guo S, Chen X, Wei Q, Wang M Biochem Biophys Res Commun. 2024 Sep 29;734:150767. doi: , 10.1016/j.bbrc.2024.150767. PMID:39366178[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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