Database accession: MF7000643
Name: CalO1 with SAH
PDB ID: 3lst
Experimental method: X-ray (2.40 Å)
Assembly: Homodimer
Source organism: Micromonospora echinospora
Primary publication of the structure:
Chang A, Singh S, Bingman CA, Thorson JS, Phillips GN
Structural characterization of CalO1: a putative orsellinic acid methyltransferase in the calicheamicin-biosynthetic pathway.
(2011) Acta Crystallogr. D Biol. Crystallogr. 67: 197-203
PMID: 21358050
Abstract:
The X-ray structure determination at 2.4 Å resolution of the putative orsellinic acid C3 O-methyltransferase (CalO1) involved in calicheamicin biosynthesis is reported. Comparison of CalO1 with a homology model of the functionally related calicheamicin orsellinic acid C2 O-methyltransferase (CalO6) implicates several residues that are likely to contribute to the regiospecificity of alkylation. Consistent with the proposed requirement of an acyl-carrier-protein-bound substrate, this structural study also reveals structural determinants within CalO1 that are anticipated to accommodate an association with an acyl carrier protein.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
O-methyltransferase activity O-methyltransferase activity
Biological process: not assigned
Cellular component: not assigned
Structural annotations of the participating protein chains.Entry contents: 2 distinct polypeptide molecules
Chains: A, A-2
Notes: All chains according to the most probable oligomerization state stored in PDBe were considered.
Number of unique protein segments: 1
Name: CalO1
Source organism: Micromonospora echinospora
Length: 345 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMQRQRPPSRAGGDMDRLQSALALYEEAMGYTYAAALRAAAAVGVADHLVDGPRTPAELAAATGTDADALRRVLRLLAVRDVVRESDGRFALTDKGAALRSDSPVPARAGILMFTDTMFWTMSHRVASALGPERPAFADIFGSSLDAYFDGDAEVEALYYEGMETVSAAEHLILARAGDFPATGTVADVGGGRGGFLLTVLREHPGLQGVLLDRAEVVARHRLDAPDVAGRWKVVEGDFLREVPHADVHVLKRILHNWGDEDSVRILTNCRRVMPAHGRVLVIDAVVPEGNDAHQSKEMDFMMLAARTGQERTAAELEPLFTAAGLRLDRVVGTSSVMSIAVGVPA
UniProtKB AC: Q8KNE5 (positions: 13-345)
Coverage: 96%
Name: CalO1
Source organism: Micromonospora echinospora
Length: 345 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMQRQRPPSRAGGDMDRLQSALALYEEAMGYTYAAALRAAAAVGVADHLVDGPRTPAELAAATGTDADALRRVLRLLAVRDVVRESDGRFALTDKGAALRSDSPVPARAGILMFTDTMFWTMSHRVASALGPERPAFADIFGSSLDAYFDGDAEVEALYYEGMETVSAAEHLILARAGDFPATGTVADVGGGRGGFLLTVLREHPGLQGVLLDRAEVVARHRLDAPDVAGRWKVVEGDFLREVPHADVHVLKRILHNWGDEDSVRILTNCRRVMPAHGRVLVIDAVVPEGNDAHQSKEMDFMMLAARTGQERTAAELEPLFTAAGLRLDRVVGTSSVMSIAVGVPA
UniProtKB AC: Q8KNE5 (positions: 13-345)
Coverage: 96%
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 A-2:
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)
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