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Crystal Structure of Bee-Venom Phospholipase A 2 in a Complex with a Transition-State Analogue
Abstract
The 2.0 angstroms crystal structure of a complex containing bee-venom phospholipase A 2 (PLA 2 ) 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 PLA 2 does not belong to the large homologous Class I/II family that encompasses most other well-studied PLA 2 s, 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.
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EAACI Molecular Allergology User's Guide
Matricardi, P. M., Kleine‐Tebbe, J., Hoffmann, H. J., Valenta, R., Hilger, C., Hofmaier, S., Aalberse, R. C., Agache, I., Asero, R., Ballmer‐Weber, B., et al. (2016) · Pediatric Allergy and Immunology · doi:10.1111/pai.12563 · Cited by 932
Cloning and expression of a membrane receptor for secretory phospholipases A2.
Lambeau, G., Ancian, P., Barhanin, J., & Lazdunski, M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42060-6 · Cited by 279
Bühring, H.-J., Streble, A., & Valent, P. (2004) · International Archives of Allergy and Immunology · doi:10.1159/000077351 · Cited by 231
Metadata
- Authors
- Scott, D. L., Otwinowski, Z., Gelb, M. H., & Sigler, P. B.
- Venue
- Science
- Published
- 1990-12-14
- Volume
- 250
- Issue
- 4987
- Pages
- 1563-1566
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2106150672
- Cited by
- 445
- References
- 0
- FWCI
- 21.25
- Type
- journal article
- Language
- en
- Open access
- closed
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- Scott, D. L., Otwinowski, Z., Gelb, M. H., & Sigler, P. B. (1990). Crystal Structure of Bee-Venom Phospholipase A 2 in a Complex with a Transition-State Analogue. Science. https://doi.org/10.1126/science.2274788
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