1POC

CRYSTAL STRUCTURE OF BEE-VENOM PHOSPHOLIPASE A2 IN A COMPLEX WITH A TRANSITION-STATE ANALOGUE

Summary for 1POC

• Entry DOI: 10.2210/pdb1poc/pdb
• Descriptor: PHOSPHOLIPASE A2, CALCIUM ION, 1-O-OCTYL-2-HEPTYLPHOSPHONYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE, ... (4 entities in total)
• Functional Keywords: hydrolase
• Biological source: Apis mellifera (honey bee)
• Total number of polymer chains: 1
• Total formula weight: 15803.92

Authors

Scott, D.L.,Otwinowski, Z.,Sigler, P.B. (deposition date: 1992-09-07, release date: 1993-10-31, Last modification date: 2024-10-30)

Primary citation

Scott, D.L.,Otwinowski, Z.,Gelb, M.H.,Sigler, P.B.
Crystal structure of bee-venom phospholipase A2 in a complex with a transition-state analogue.
Science, 250:1563-1566, 1990

PubMed Abstract: The 2.0 angstroms crystal structure of a complex containing bee-venom phospholipase A2 (PLA2) and a phosphonate transition-state analogue was solved by multiple isomorphous replacement. The electron-density map is sufficiently detailed to visualize the proximal sugars of the enzyme's N-linked carbohydrate and a single molecule of the transition-state analogue bound ot its active center. Although bee-venom PLA2 does not belong to the large homologous Class I/II family that encompasses most other well-studied PLA2s, there is segmental sequence similarity and conservation of many functional substructures. Comparison of the bee-venom enzyme with other phospholipase structures provides compelling evidence for a common catalytic mechanism.

PubMed: 2274788

Experimental method

X-RAY DIFFRACTION (2 Å)