5kva

Crystal Structure of sorghum caffeoyl-CoA O-methyltransferase (CCoAOMT)

spinqualitylabelsall models 5kva, resolution 1.83Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5kva is a 2 chain structure with sequence from Sorghum bicolor. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.827Å Ligands: CA, SAM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C5Z4W3_SORBI Publication Abstract from PubMed Caffeoyl-CoA 3-O-methyltransferase (CCoAOMT) is an S-adenosyl methionine (SAM)-dependent O-methyltransferase responsible for methylation of the meta-hydroxyl group of caffeoyl-CoA, on the pathway to monolignols with their ring methoxylation status characteristic of guaiacyl or syringyl units in lignin. In order to better understand the unique class of type-2 O-methyltransferases from monocots, we have characterized CCoAOMT from sorghum (Sorghum bicolor) (SbCCoAOMT), including the SAM binary complex crystal structure, steady state enzyme kinetics, isothermal titration calorimetry (ITC), inductively coupled plasma-optical emission spectroscopy (ICP-OES) and molecular docking. Key amino acid residues were validated with site-directed mutagenesis. ITC data indicated a sequential binding mechanism for SbCCoAOMT, wherein SAM binds prior to caffeoyl-CoA, and the enzyme showed allosteric behavior with respect to it. 5-Hydroxyferuloyl-CoA was not a substrate for SbCCoAOMT. We propose a catalytic mechanism in which Lys180 acts as a catalytic base and deprotonates the reactive hydroxyl group of caffeoyl-CoA. This deprotonation is facilitated by the coordination of the reactive hydroxyl group by Ca2+ in the active site, lowering the pKa of the 3'-OH group. Collectively, these data give a new perspective on the catalytic mechanism of CCoAOMTs and provide a basis for the functional diversity exhibited by type-2 plant OMTs that contain a unique insertion loop (residues 208-231) conferring affinity for phenylpropanoid-CoA thioesters. Determination of the structure and catalytic mechanism of Sorghum bicolor caffeoyl-CoA O-methyltransferase.,Walker AM, Sattler SA, Regner MR, Jones JP, Ralph J, Vermerris W, Sattler SE, Kang C Plant Physiol. 2016 Jul 25. pii: pp.00845.2016. PMID:27457122 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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