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The active site of aspartic proteinases
Open accessAbstract
The active site of the aspartic proteinase, endothiapepsin, has been defined by X‐ray analysis and restrained least‐squares refinement at 2.1 Å resolution with a crystallographic agreement value of 0.16. The environments of the two catalytically important aspartyl groups are remarkably similar and the contributions of the NH 2‐ and COOH‐terminal domains to the catalytic centre are related by a local 2‐fold axis. The carboxylates of the aspartyls share a hydrogen bond and have equivalent contacts to a bound water molecule or hydroxonium ion lying on the local diad. The main chains around 32 and 215 are connected by a novel interaction involving diad‐related threonines. It is suggested that the two p K a, values of the active site aspartyls arise from a structure not unlike that in maleic acid with a hydrogen‐bonded intermediate species and a dicarboxylate characterised by electrostatic repulsions between the two negatively charged groups.
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Cited by
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Retroviral proteases and their roles in virion maturation
Konvalinka, J., Kräusslich, H.-G., & Müller, B. (2015) · Virology · doi:10.1016/j.virol.2015.03.021 · Cited by 148
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Metadata
- Authors
- Pearl, L., & Blundell, T.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1984-08-20
- Volume
- 174
- Issue
- 1
- Pages
- 96-101
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2128827201
- Cited by
- 263
- References
- 0
- FWCI
- 14.18
- Type
- journal article
- Language
- en
- Open access
- bronze
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