Database accession: MF7000644
Name: Coniferyl Alcohol 9-O-Methyltransferase with coniferyl alcohol (Linum Nodiflorum)
PDB ID: 4e70
Experimental method: X-ray (1.61 Å)
Assembly: Homodimer
Source organism: Linum nodiflorum
Primary publication of the structure:
Wolters S, Neeb M, Berim A, Schulze Wischeler J, Petersen M, Heine A
Structural analysis of coniferyl alcohol 9-O-methyltransferase from Linum nodiflorum reveals a novel active-site environment.
(2013) Acta Crystallogr. D Biol. Crystallogr. 69: 888-900
PMID: 23633600
Abstract:
Coniferyl alcohol 9-O-methyltransferase from Linum nodiflorum (Linaceae) catalyzes the unusual methylation of the side-chain hydroxyl group of coniferyl alcohol. The protein was heterologously expressed in Escherichia coli as a hexahistidine derivative and purified for crystallization. Diffracting crystals were obtained of the pure protein and of its selenomethionine derivative, as well as of complexes with coniferyl alcohol and with S-adenosyl-L-homocysteine together with coniferyl alcohol 9-O-methyl ether (PDB entries 4ems, 4e70 and 4evi, respectively). The X-ray structures show that the phenylpropanoid binding mode differs from other phenylpropanoid O-methyltransferases such as caffeic acid O-methyltransferase. Moreover, the active site lacks the usually conserved and catalytic histidine residue and thus implies a different reaction mode for methylation. Site-directed mutagenesis was carried out to identify critical amino acids. The binding order of coniferyl alcohol and S-adenosyl-L-methionine was investigated by isothermal titration calorimetry experiments.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
acetylserotonin O-methyltransferase activity acetylserotonin O-methyltransferase activity
protein dimerization activity protein dimerization activity
Biological process:
melatonin biosynthetic process melatonin biosynthetic process
methylation methylation
Cellular component: not assigned
Structural annotations of the participating protein chains.Entry contents: 2 distinct polypeptide molecules
Chains: A, B
Notes: All chains according to the most probable oligomerization state stored in PDBe were considered.
Number of unique protein segments: 1
Name: Coniferyl alcohol 9-O-methyltransferase
Source organism: Linum nodiflorum
Length: 368 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMDAATAVELLDAQPQVWHHFLGYINSMTLQCALELDIADVIHRHGHPIPLNQLAAALEIPQTKAPFLSRLMRMLVHLGYFTQVITKPEDENDDVLPSYWLAPLSRLLLKQNPYNARSLTFCSVHEHLVDPWRQMSAWLRTGKEDGKDTPNAFAFAHEGKKVYEVCSEDANFSQLFSEGMAGDSWLFSRALVSKCRDAFEGLSSLVDVGGGTGNTSKVIAETFPNIHCTVFDLPHVVSGPKQTHPNLDYESGNMFTDEIPHADAVLFKWVLCDWPDEPVLKMLKQCKKALTKNGVKGKLMIADHVLDHESCNDSNSMGTSLILDMLFMSFLEGSLRTEKQWAKLFAEAGFKDYKITPVGGLRVLIEVYP
UniProtKB AC: A6XNE6 (positions: 1-368)
Coverage: 100%
Name: Coniferyl alcohol 9-O-methyltransferase
Source organism: Linum nodiflorum
Length: 368 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMDAATAVELLDAQPQVWHHFLGYINSMTLQCALELDIADVIHRHGHPIPLNQLAAALEIPQTKAPFLSRLMRMLVHLGYFTQVITKPEDENDDVLPSYWLAPLSRLLLKQNPYNARSLTFCSVHEHLVDPWRQMSAWLRTGKEDGKDTPNAFAFAHEGKKVYEVCSEDANFSQLFSEGMAGDSWLFSRALVSKCRDAFEGLSSLVDVGGGTGNTSKVIAETFPNIHCTVFDLPHVVSGPKQTHPNLDYESGNMFTDEIPHADAVLFKWVLCDWPDEPVLKMLKQCKKALTKNGVKGKLMIADHVLDHESCNDSNSMGTSLILDMLFMSFLEGSLRTEKQWAKLFAEAGFKDYKITPVGGLRVLIEVYP
UniProtKB AC: A6XNE6 (positions: 1-368)
Coverage: 100%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: Dimeric O-methyltransferase
Evidence level: Indirect evidence
Evidence coverage: Only some parts of the structure participates in mutual synergistic folding.
Complex Evidence:
Coniferyl alcohol 9-O-methyltransferase has an intertwined dimeric structure with large relative interaction surface. The active site is formed by both monomers and thus dimerization is critical for activity. The N-terminal helices form the dimerization subdomain and at the same time form the rear wall of the active-site cavity in the neighbouring monomer (PMID:23633600). Other 9-O-methyltransferase structures show similar features and exhibit no monomeric form in solution (PMID:11224575).
Chain A:
N/A
Chain B:
N/A
Surface and contacts features:
Structures from the PDB that contain the same number of proteins, and the proteins from the two structures show a sufficient degree of pairwise similarity, i.e. they belong to the same UniRef90 cluster (the full proteins exhibit at least 90% sequence identity) and convey roughly the same region to their respective interactions (the two regions from the two proteins share a minimum of 70% overlap). Download the CIF file (.cif)
Download this entry's XML file (.xml)
Download this entry's JSON file (.json)
