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PDBsum entry 1d2k
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The X-Ray structure of a chitinase from the pathogenic fungus coccidioides immitis.
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Authors
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T.Hollis,
A.F.Monzingo,
K.Bortone,
S.Ernst,
R.Cox,
J.D.Robertus.
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Ref.
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Protein Sci, 2000,
9,
544-551.
[DOI no: ]
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PubMed id
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Abstract
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The X-ray structure of chitinase from the fungal pathogen Coccidioides immitis
has been solved to 2.2 A resolution. Like other members of the class 18
hydrolase family, this 427 residue protein is an eight-stranded
beta/alpha-barrel. Although lacking an N-terminal chitin anchoring domain, the
enzyme closely resembles the chitinase from Serratia marcescens. Among the
conserved features are three cis peptide bonds, all involving conserved active
site residues. The active site is formed from conserved residues such as
tryptophans 47, 131, 315, 378, tyrosines 239 and 293, and arginines 52 and 295.
Glu171 is the catalytic acid in the hydrolytic mechanism; it was mutated to a
Gln, and activity was abolished. Allosamidin is a substrate analog that strongly
inhibits the class 18 enzymes. Its binding to the chitinase hevamine has been
observed, and we used conserved structural features of the two enzymes to
predict the inhibitors binding to the fungal enzyme.
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Secondary reference #1
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Title
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Crystallization and preliminary X-Ray analysis of a chitinase from the fungal pathogen coccidioides immitis.
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Authors
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T.Hollis,
A.F.Monzingo,
K.Bortone,
E.Schelp,
R.Cox,
J.D.Robertus.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1998,
54,
1412-1413.
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PubMed id
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