1gdu
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FUSARIUM OXYSPORUM TRYPSIN AT ATOMIC RESOLUTION
OverviewOverview
The X-ray structure of F. oxysporum trypsin has been determined at atomic, resolution, revealing electron density in the binding site which was, interpreted as a peptide bound in the sites S1, S2 and S3. The structure, which was initially determined at 1.07 A resolution and 283 K, has an Arg, in the S1 specificity pocket. The study was extended to 0.81 A resolution, at 100 K using crystals soaked in Arg, Lys and Gln to study in greater, detail the binding at the S1 site. The electron density in the binding, site was compared between the different structures and analysed in terms, of partially occupied and overlapping components of peptide, solvent water, and possibly other chemical moieties. Arg-soaked crystals reveal a density, more detailed but similar to the original structure, with the Arg side, chain visible in the S1 pocket and residual peptide density in the S2 and, S3 sites. The density in the active site is complex and not fully, interpreted. Lys at high concentrations displaces Arg in the S1 pocket, while some main-chain density remains in sites S2 and S3. Gln has been, shown not to bind. The free peptide in the S1-S3 sites binds in a similar, way to the binding loop of BPTI or the inhibitory domain of the, Alzheimer's beta-protein precursor, with some differences in the S1 site.
About this StructureAbout this Structure
1GDU is a Single protein structure of sequence from Fusarium oxysporum with SO4 as ligand. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.
ReferenceReference
Fusarium oxysporum trypsin at atomic resolution at 100 and 283 K: a study of ligand binding., Rypniewski WR, Ostergaard PR, Norregaard-Madsen M, Dauter M, Wilson KS, Acta Crystallogr D Biol Crystallogr. 2001 Jan;57(Pt 1):8-19. PMID:11134922
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