5LOG

Crystal Structure of SafC from Myxococcus xanthus bound to SAM

Summary for 5LOG

• Entry DOI: 10.2210/pdb5log/pdb
• Descriptor: Putative O-methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: o-methyl transferase, sam, transferase
• Biological source: Myxococcus xanthus
• Total number of polymer chains: 2
• Total formula weight: 53147.58

Authors

Gerhardt, S.,Netzer, J.,Einsle, O. (deposition date: 2016-08-09, release date: 2017-06-21, Last modification date: 2024-01-10)

Primary citation

Siegrist, J.,Netzer, J.,Mordhorst, S.,Karst, L.,Gerhardt, S.,Einsle, O.,Richter, M.,Andexer, J.N.
Functional and structural characterisation of a bacterial O-methyltransferase and factors determining regioselectivity.
FEBS Lett., 591:312-321, 2017

PubMed Abstract: Mg -dependent catechol-O-methyltransferases occur in animals as well as in bacteria, fungi and plants, often with a pronounced selectivity towards one of the substrate's hydroxyl groups. Here, we show that the bacterial MxSafC exhibits excellent regioselectivity for para as well as for meta methylation, depending on the substrate's characteristics. The crystal structure of MxSafC was solved in apo and in holo form. The structure complexed with a full set of substrates clearly illustrates the plasticity of the active site region. The awareness that a wide range of factors influences the regioselectivity will aid the further development of catechol-O-methyltransferases as well as other methyltransferases as selective and efficient biocatalysts for chemical synthesis.

PubMed: 27990630
DOI: 10.1002/1873-3468.12530

Experimental method

X-RAY DIFFRACTION (2.01 Å)