2VNE
The X-ray structure of Norcoclaurine synthase from Thalictrum flavum
Summary for 2VNE
| Entry DOI | 10.2210/pdb2vne/pdb |
| Related | 2VQ5 |
| Descriptor | S-NORCOCLAURINE SYNTHASE (2 entities in total) |
| Functional Keywords | lyase, norcoclaurine synthase, biosynthesis of benzylisoquinoline alkaloids |
| Biological source | THALICTRUM FLAVUM |
| Total number of polymer chains | 2 |
| Total formula weight | 45212.42 |
| Authors | Ilari, A.,Franceschini, S.,Boffi, A.,Bonamore, A.,Pasquo, A. (deposition date: 2008-02-04, release date: 2008-08-05, Last modification date: 2024-10-23) |
| Primary citation | Ilari, A.,Franceschini, S.,Bonamore, A.,Arenghi, F.,Botta, B.,Macone, A.,Pasquo, A.,Bellucci, L.,Boffi, A. Structural Basis of Enzymatic S-Norcoclaurine Biosynthesis. J.Biol.Chem., 284:897-, 2009 Cited by PubMed Abstract: The enzyme norcoclaurine synthase (NCS) catalyzes the stereospecific Pictet-Spengler cyclization between dopamine and 4-hydroxyphenylacetaldehyde, the key step in the benzylisoquinoline alkaloid biosynthetic pathway. The crystallographic structure of norcoclaurine synthase from Thalictrum flavum in its complex with dopamine substrate and the nonreactive substrate analogue 4-hydroxybenzaldehyde has been solved at 2.1A resolution. NCS shares no common features with the functionally correlated "Pictet-Spenglerases" that catalyze the first step of the indole alkaloids pathways and conforms to the overall fold of the Bet v1-like protein. The active site of NCS is located within a 20-A-long catalytic tunnel and is shaped by the side chains of a tyrosine, a lysine, an aspartic, and a glutamic acid. The geometry of the amino acid side chains with respect to the substrates reveals the structural determinants that govern the mechanism of the stereoselective Pictet-Spengler cyclization, thus establishing an excellent foundation for the understanding of the finer details of the catalytic process. Site-directed mutations of the relevant residues confirm the assignment based on crystallographic findings. PubMed: 19004827DOI: 10.1074/JBC.M803738200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.72 Å) |
Structure validation
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