1D2K

C. IMMITIS CHITINASE 1 AT 2.2 ANGSTROMS RESOLUTION

Summary for 1D2K

• Entry DOI: 10.2210/pdb1d2k/pdb
• Descriptor: CHITINASE 1 (2 entities in total)
• Functional Keywords: beta-alpha barrel, hydrolase
• Biological source: Coccidioides immitis
• Total number of polymer chains: 1
• Total formula weight: 43714.81

Authors

Hollis, T.,Monzingo, A.F.,Bortone, K.,Ernst, S.R.,Cox, R.,Robertus, J.D. (deposition date: 1999-09-23, release date: 2000-09-27, Last modification date: 2024-02-07)

Primary citation

Hollis, T.,Monzingo, A.F.,Bortone, K.,Ernst, S.,Cox, R.,Robertus, J.D.
The X-ray structure of a chitinase from the pathogenic fungus Coccidioides immitis.
Protein Sci., 9:544-551, 2000

PubMed Abstract: 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.

PubMed: 10752616

Experimental method

X-RAY DIFFRACTION (2.2 Å)