1try: Difference between revisions
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|PDB= 1try |SIZE=350|CAPTION= <scene name='initialview01'>1try</scene>, resolution 1.55Å | |PDB= 1try |SIZE=350|CAPTION= <scene name='initialview01'>1try</scene>, resolution 1.55Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=ISP:PHOSPHORYLISOPROPANE'>ISP</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1try FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1try OCA], [http://www.ebi.ac.uk/pdbsum/1try PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1try RCSB]</span> | |||
}} | }} | ||
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[[Category: Rypniewski, W R.]] | [[Category: Rypniewski, W R.]] | ||
[[Category: Wilson, K S.]] | [[Category: Wilson, K S.]] | ||
[[Category: hydrolase (serine proteinase)]] | [[Category: hydrolase (serine proteinase)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:00:19 2008'' | ||
Revision as of 00:00, 31 March 2008
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| , resolution 1.55Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Trypsin, with EC number 3.4.21.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF INHIBITED TRYPSIN FROM FUSARIUM OXYSPORUM AT 1.55 ANGSTROMS
OverviewOverview
The structure of trypsin from the fungus Fusarium oxysporum has been refined at 1.55 A resolution by restrained least-squares minimization to an R-factor of 14.4%. The data were recorded from a single-crystal on the X31 beamline at EMBL, Hamburg, using a locally developed image-plate scanner. The final model consists of 1557 protein atoms, 400 water molecules, one molecule of isopropanol and one monoisopropyl phosphoryl inhibitor group covalently bound to the catalytic Ser195. Comparison of the structure with bovine trypsin reveals significant differences in the active site and suggests a possible explanation for the difference in substrate specificity between the two enzymes. In F. oxysporum trypsin the specificity pocket is larger than in bovine trypsin. This explains the preference of F. oxysporum trypsin for the bulkier arginine over lysine and the reverse preference in bovine trypsin. The binding cavity on the C-terminal side of the substrate is more restricted in F. oxysporum trypsin than in mammalian and Streptomyces griseus trypsins, which explains the relative inactivity of F. oxysporum trypsin towards peptide-pNA substrate analogues as an unfavourable steric interaction between the side of the binding cavity and the para-nitroanilino group of peptide-pNA. The observed restriction of the binding cavity does not lead to a reduced catalytic activity compared to other trypsins.
About this StructureAbout this Structure
1TRY is a Single protein structure of sequence from Fusarium oxysporum. Full crystallographic information is available from OCA.
ReferenceReference
Structure of inhibited trypsin from Fusarium oxysporum at 1.55 A., Rypniewski WR, Dambmann C, von der Osten C, Dauter M, Wilson KS, Acta Crystallogr D Biol Crystallogr. 1995 Jan 1;51(Pt 1):73-85. PMID:15299338
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