5log

Crystal Structure of SafC from Myxococcus xanthus bound to SAM

spinqualitylabelsall models 5log, resolution 2.01Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5log is a 2 chain structure with sequence from Myxococcus xanthus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.01Å Ligands: CL, LDP, MG, SAH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q50859_MYXXA Publication Abstract from PubMed Mg2+ -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. Functional and structural characterisation of a bacterial O-methyltransferase and factors determining regioselectivity.,Siegrist J, Netzer J, Mordhorst S, Karst L, Gerhardt S, Einsle O, Richter M, Andexer JN FEBS Lett. 2017 Jan;591(2):312-321. doi: 10.1002/1873-3468.12530. Epub 2017 Jan, 8. PMID:27990630 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA