1try: Difference between revisions

Revision as of 13:33, 27 July 2008

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File:1try.png

Template:STRUCTURE 1try

STRUCTURE OF INHIBITED TRYPSIN FROM FUSARIUM OXYSPORUM AT 1.55 ANGSTROMSSTRUCTURE OF INHIBITED TRYPSIN FROM FUSARIUM OXYSPORUM AT 1.55 ANGSTROMS

Template:ABSTRACT PUBMED 15299338

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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-[[Image:1try.gif|left|200px]]
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-'''STRUCTURE OF INHIBITED TRYPSIN FROM FUSARIUM OXYSPORUM AT 1.55 ANGSTROMS'''
+===STRUCTURE OF INHIBITED TRYPSIN FROM FUSARIUM OXYSPORUM AT 1.55 ANGSTROMS===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15299338}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15299338 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15299338}}
 ==About this Structure==
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 [[Category: Rypniewski, W R.]]
 [[Category: Wilson, K S.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:18:07 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:33:11 2008''