1SUI
Alfalfa caffeoyl coenzyme A 3-O-methyltransferase
Summary for 1SUI
| Entry DOI | 10.2210/pdb1sui/pdb |
| Related | 1SUS |
| Descriptor | Caffeoyl-CoA O-methyltransferase, CALCIUM ION, S-ADENOSYL-L-HOMOCYSTEINE, ... (5 entities in total) |
| Functional Keywords | rossmann fold, protein-cofactor-substrate complex, transferase |
| Biological source | Medicago sativa |
| Total number of polymer chains | 4 |
| Total formula weight | 114802.37 |
| Authors | Ferrer, J.-L.,Zubieta, C.,Dixon, R.A.,Noel, J.P. (deposition date: 2004-03-26, release date: 2005-03-15, Last modification date: 2024-02-14) |
| Primary citation | Ferrer, J.-L.,Zubieta, C.,Dixon, R.A.,Noel, J.P. Crystal Structures of Alfalfa Caffeoyl Coenzyme A 3-O-Methyltransferase Plant Physiol., 137:1009-1017, 2005 Cited by PubMed Abstract: Caffeoyl coenzyme A 3-O-methyltransferases (CCoAOMTs) are S-adenosyl-l-methionine-dependent O-methyltransferases (OMTs) involved in lignin biosynthesis. Plant CCoAOMTs belong to a distinct family of OMTs, more closely related to the mammalian catechol OMTs than to other plant OMTs. The crystal structure of alfalfa (Medicago sativa) CCoAOMT in complex with the reaction products S-adenosine-l-homocysteine and feruloyl/sinapoyl CoAs presented here belong to a structurally and mechanistically distinct family of plant small molecule OMTs. These structures provide a new understanding of the substrate preferences and the catalytic mechanism accompanying CCoAOMT-mediated O-methylation of CoA-linked phenylpropanoid substrates. PubMed: 15734921DOI: 10.1104/pp.104.048751 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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