ArticleProtein science : a publication of the Protein Society2001
Structural investigations of the active-site mutant Asn156Ala of outer membrane phospholipase A: function of the Asn-His interaction in the catalytic triad.
Article in Protein science : a publication of the Protein Society, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 14 citations in OpenAlex.
- Protein sequence optimization with a pairwise decomposable penalty for buried unsatisfied hydrogen bonds.PLoS computational biology · 2021Article
- Structural and functional insights into caseinolytic proteases reveal an unprecedented regulation principle of their catalytic triad.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- PagP crystallized from SDS/cosolvent reveals the route for phospholipid access to the hydrocarbon ruler.Structure (London, England : 1993) · 2010Article
- Structural biology of membrane-intrinsic beta-barrel enzymes: sentinels of the bacterial outer membrane.Biochimica et biophysica acta · 2008Review
- Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
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Authors and funding
7 authors at 2 institutions in 1 country.
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Abstract
Outer membrane phospholipase A (OMPLA) from Escherichia coli is an integral-membrane enzyme with a unique His-Ser-Asn catalytic triad. In serine proteases and serine esterases usually an Asp occurs in the catalytic triad; its role has been the subject of much debate. Here the role of the uncharged asparagine in the active site of OMPLA is investigated by structural characterization of the Asn156Ala mutant. Asparagine 156 is not involved in maintaining the overall active-site configuration and does not contribute significantly to the thermal stability of OMPLA. The active-site histidine retains an active conformation in the mutant notwithstanding the loss of the hydrogen bond to the asparagine side chain. Instead, stabilization of the correct tautomeric form of the histidine can account for the observed decrease in activity of the Asn156Ala mutant.
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