2WFL

Crystal structure of polyneuridine aldehyde esterase

Summary for 2WFL

• Entry DOI: 10.2210/pdb2wfl/pdb
• Related: 2WFM
• Descriptor: POLYNEURIDINE-ALDEHYDE ESTERASE, SULFATE ION, ... (4 entities in total)
• Functional Keywords: alkaloid metabolism, monoterpenoid indole alkaloids, pnae, hydrolase, serine esterase
• Biological source: RAUVOLFIA SERPENTINA (SERPENTWOOD); More
• Total number of polymer chains: 2
• Total formula weight: 59803.23

Authors

Yang, L.,Hill, M.,Panjikar, S.,Wang, M.,Stoeckigt, J. (deposition date: 2009-04-08, release date: 2009-08-18, Last modification date: 2024-11-13)

Primary citation

Yang, L.,Hill, M.,Wang, M.,Panjikar, S.,Stockigt, J.
Structural Basis and Enzymatic Mechanism of the Biosynthesis of C9- from C10-Monoterpenoid Indole Alkaloids.
Angew.Chem.Int.Ed.Engl., 48:5211-, 2009

PubMed Abstract: Cutting carbons: The three-dimensional structure of polyneuridine aldehyde esterase (PNAE) gives insight into the enzymatic mechanism of the biosynthesis of C(9)- from C(10)-monoterpenoid indole alkaloids (see scheme). PNAE is a very substrate-specific serine esterase. It harbors the catalytic triad S87-D216-H244, and is a new member of the alpha/beta-fold hydrolase superfamily. Its novel function leads to the diversification of alkaloid structures.

PubMed: 19496101
DOI: 10.1002/ANIE.200900150

Experimental method

X-RAY DIFFRACTION (2.1 Å)