1d2k
C. IMMITIS CHITINASE 1 AT 2.2 ANGSTROMS RESOLUTION
OverviewOverview
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.
About this StructureAbout this Structure
1D2K is a Single protein structure of sequence from Coccidioides immitis. Full crystallographic information is available from OCA.
ReferenceReference
The X-ray structure of a chitinase from the pathogenic fungus Coccidioides immitis., Hollis T, Monzingo AF, Bortone K, Ernst S, Cox R, Robertus JD, Protein Sci. 2000 Mar;9(3):544-51. PMID:10752616 Page seeded by OCA on Fri May 2 13:22:35 2008