Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA
Article Abstract:
Research revealing the crystal structure of a complex of the trp RNA-binding attenuation protein and a 53-base single-stranded RNA containing 11 GAG triplets indicates that the recognition of single-stranded RNA does not necessarily involve protein interactions with the phosphates of RNA. Furthermore, the structure indicates that some RNA segments are bound to protein with the same conformational angles that arise in the A-form double helix. This suggests that TRAP may choose from the nascent RNA transcript the conformation likely to predominate before binding.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
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+A protein catalytic framework with an N-terminal nucleophile is capable of self-activation
Article Abstract:
Three enzymes and their capability for autocatalytic activation and engaging in nucleophilic attack are discussed. These three are glutamine PRPP amidotransferase, penicillin acylase and poteasome. They occupy a common fold that enables them to perform similar activities although they look divergent enough to mask their common evolutionary pattern and origin. A suggested name for this set of enzymes is Ntn hydrolases.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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Penicillin acylase has a single-amino-acid catalytic centre
Article Abstract:
The crystal structure of penicillin acylase is determined at a resolution of 1.9 angstroms by using multiple isomorphous replacement technique. The crystal structure reveals that there are no adjacent histidine type molecules near the catalytically active N-terminal serine of the B-chain. The serine region has an alpha-amino group which provides the penicillin acylase enzyme with its catalytic properties.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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