1ild: Difference between revisions
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'''OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE MUTANT pH 4.6''' | '''OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE MUTANT pH 4.6''' | ||
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Structural investigations of the active-site mutant Asn156Ala of outer membrane phospholipase A: function of the Asn-His interaction in the catalytic triad., Snijder HJ, Van Eerde JH, Kingma RL, Kalk KH, Dekker N, Egmond MR, Dijkstra BW, Protein Sci. 2001 Oct;10(10):1962-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11567087 11567087] | Structural investigations of the active-site mutant Asn156Ala of outer membrane phospholipase A: function of the Asn-His interaction in the catalytic triad., Snijder HJ, Van Eerde JH, Kingma RL, Kalk KH, Dekker N, Egmond MR, Dijkstra BW, Protein Sci. 2001 Oct;10(10):1962-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11567087 11567087] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dekker, N.]] | [[Category: Dekker, N.]] | ||
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[[Category: Kingma, R L.]] | [[Category: Kingma, R L.]] | ||
[[Category: Snijder, H J.]] | [[Category: Snijder, H J.]] | ||
[[Category: | [[Category: Anti-parallel beta barrel]] | ||
[[Category: | [[Category: Membrane phospholipase]] | ||
[[Category: | [[Category: Membrane protein]] | ||
[[Category: | [[Category: N156a]] | ||
[[Category: | [[Category: Serine hydrolase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:07:28 2008'' | |||
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Revision as of 20:07, 2 May 2008
OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE MUTANT pH 4.6
OverviewOverview
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.
About this StructureAbout this Structure
1ILD is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Structural investigations of the active-site mutant Asn156Ala of outer membrane phospholipase A: function of the Asn-His interaction in the catalytic triad., Snijder HJ, Van Eerde JH, Kingma RL, Kalk KH, Dekker N, Egmond MR, Dijkstra BW, Protein Sci. 2001 Oct;10(10):1962-9. PMID:11567087 Page seeded by OCA on Fri May 2 20:07:28 2008