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1try

From Proteopedia

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(New page: 200px<br /><applet load="1try" size="450" color="white" frame="true" align="right" spinBox="true" caption="1try, resolution 1.55&Aring;" /> '''STRUCTURE OF INHIBIT...)
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[[Image:1try.gif|left|200px]]<br /><applet load="1try" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1try, resolution 1.55&Aring;" />
 
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'''STRUCTURE OF INHIBITED TRYPSIN FROM FUSARIUM OXYSPORUM AT 1.55 ANGSTROMS'''<br />
 
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==Overview==
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==STRUCTURE OF INHIBITED TRYPSIN FROM FUSARIUM OXYSPORUM AT 1.55 ANGSTROMS==
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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.
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<StructureSection load='1try' size='340' side='right'caption='[[1try]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1try]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusarium_oxysporum Fusarium oxysporum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TRY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TRY FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=ISP:PHOSPHORYLISOPROPANE'>ISP</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1try FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1try OCA], [https://pdbe.org/1try PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1try RCSB], [https://www.ebi.ac.uk/pdbsum/1try PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1try ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TRYP_FUSOX TRYP_FUSOX]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tr/1try_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1try ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1TRY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_oxysporum Fusarium oxysporum] with ISP and IPA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TRY OCA].
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*[[Trypsin 3D structures|Trypsin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299338 15299338]
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[[Category: Fusarium oxysporum]]
[[Category: Fusarium oxysporum]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Trypsin]]
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[[Category: Dambmann C]]
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[[Category: Dambmann, C.]]
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[[Category: Dauter M]]
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[[Category: Dauter, M.]]
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[[Category: Rypniewski WR]]
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[[Category: Osten, C.Von.Der.]]
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[[Category: Von Der Osten C]]
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[[Category: Rypniewski, W.R.]]
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[[Category: Wilson KS]]
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[[Category: Wilson, K.S.]]
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[[Category: IPA]]
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[[Category: ISP]]
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[[Category: hydrolase (serine proteinase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:32:51 2007''
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Current revision

STRUCTURE OF INHIBITED TRYPSIN FROM FUSARIUM OXYSPORUM AT 1.55 ANGSTROMS

PDB ID 1try

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