1im0

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[[Image:1im0.jpg|left|200px]]
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{{Seed}}
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[[Image:1im0.png|left|200px]]
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{{STRUCTURE_1im0| PDB=1im0 | SCENE= }}
{{STRUCTURE_1im0| PDB=1im0 | SCENE= }}
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'''OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE MUTANT PH 8.3'''
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===OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE MUTANT PH 8.3===
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==Overview==
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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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The line below this paragraph, {{ABSTRACT_PUBMED_11567087}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 11567087 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11567087}}
==About this Structure==
==About this Structure==
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[[Category: Membrane protein]]
[[Category: Membrane protein]]
[[Category: Serine hydrolase]]
[[Category: Serine hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:08:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 13:30:12 2008''

Revision as of 10:30, 1 July 2008

Image:1im0.png

Template:STRUCTURE 1im0

OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE MUTANT PH 8.3

Template:ABSTRACT PUBMED 11567087

About this Structure

1IM0 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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

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