5tl4

Crystal structure of Sphingomonas paucimobilis aryl O-demethylase LigMCrystal structure of Sphingomonas paucimobilis aryl O-demethylase LigM

Structural highlights

5tl4 is a 4 chain structure with sequence from Sphingomonas paucimobilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.751Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LIGM_SPHSK Involved in the catabolism of vanillate and syringate. Catalyzes the transfer of a methyl moiety from vanillate or 3-O-methylgallate (3MGA) to tetrahydrofolate, forming protocatechuate (PCA) or gallate, respectively, and methyl-tetrahydrofolate. Has similar activities with both substrates (PubMed:15743951). Cannot use syringate (PubMed:15743951). Uses an ordered, sequential kinetic mechanism (PubMed:28373573).^[1] ^[2]

References

↑ Abe T, Masai E, Miyauchi K, Katayama Y, Fukuda M. A tetrahydrofolate-dependent O-demethylase, LigM, is crucial for catabolism of vanillate and syringate in Sphingomonas paucimobilis SYK-6. J Bacteriol. 2005 Mar;187(6):2030-7. PMID:15743951 doi:10.1128/JB.187.6.2030-2037.2005
↑ Kohler AC, Mills MJ, Adams PD, Simmons BA, Sale KL. Structure of aryl O-demethylase offers molecular insight into a catalytic tyrosine-dependent mechanism. Proc Natl Acad Sci U S A. 2017 Apr 3. pii: 201619263. doi:, 10.1073/pnas.1619263114. PMID:28373573 doi:http://dx.doi.org/10.1073/pnas.1619263114

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OCA

[1] Abe T, Masai E, Miyauchi K, Katayama Y, Fukuda M. A tetrahydrofolate-dependent O-demethylase, LigM, is crucial for catabolism of vanillate and syringate in Sphingomonas paucimobilis SYK-6. J Bacteriol. 2005 Mar;187(6):2030-7. PMID:15743951 doi:10.1128/JB.187.6.2030-2037.2005

[2] Kohler AC, Mills MJ, Adams PD, Simmons BA, Sale KL. Structure of aryl O-demethylase offers molecular insight into a catalytic tyrosine-dependent mechanism. Proc Natl Acad Sci U S A. 2017 Apr 3. pii: 201619263. doi:, 10.1073/pnas.1619263114. PMID:28373573 doi:http://dx.doi.org/10.1073/pnas.1619263114

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