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Structure paper

TitleStructural investigations of the active-site mutant Asn156Ala of outer membrane phospholipase A: function of the Asn-His interaction in the catalytic triad.
Journal, issue, pagesProtein Sci., Vol. 10, Page 1962-1969, Year 2001
Publish dateMay 8, 2001 (structure data deposition date)
AuthorsSnijder, H.J. / Van Eerde, J.H. / Kingma, R.L. / Kalk, K.H. / Dekker, N. / Egmond, M.R. / Dijkstra, B.W.
External linksProtein Sci. / PubMed:11567087
MethodsX-ray diffraction
Resolution2.5 - 2.98 Å
Structure data

PDB-1ild:
OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE MUTANT pH 4.6
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-1ilz:
OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE MUTANT pH 6.1
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-1im0:
OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI N156A ACTIVE SITE MUTANT PH 8.3
Method: X-RAY DIFFRACTION / Resolution: 2.98 Å

Chemicals

ChemComp-BOG:
octyl beta-D-glucopyranoside / detergent*YM

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL / precipitant*YM

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / MEMBRANE PROTEIN / ANTI-PARALLEL BETA BARREL / MEMBRANE PHOSPHOLIPASE / SERINE HYDROLASE / N156A / CATALYTIC TRIAD / ASN ALA MUTATION

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