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1fy8

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(New page: 200px<br /><applet load="1fy8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fy8, resolution 1.7&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1fy8.jpg|left|200px]]<br /><applet load="1fy8" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fy8, resolution 1.7&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE DELTAILE16VAL17 RAT ANIONIC TRYPSINOGEN-BPTI COMPLEX'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE DELTAILE16VAL17 RAT ANIONIC TRYPSINOGEN-BPTI COMPLEX==
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The contribution of induced fit to enzyme specificity has been much, debated, although with little experimental data. Here we probe the effect, of induced fit on enzyme specificity using the trypsin(ogen) system. BPTI, is known to induce trypsinogen to assume a trypsinlike conformation., Correlations are observed between BPTI affinity and the values of, k(cat)/K(m) for the hydrolysis of two substrates by eight trypsin(ogen), variants. The slope of both correlations is -1.8. The crystal structures, of the BPTI complexes of four variant trypsinogens were also solved. Three, of these enzymes, K15A, DeltaI16V17/D194N, and DeltaI16V17/Q156K, trypsinogen, are 10- to 100-fold more active than trypsinogen. The fourth, variant, DeltaI16V17 trypsinogen, is the lone outlier in the correlations;, its activity is lower than expected based on its affinity for BPTI. The S1, site and oxyanion hole, formed by segments 184A-194 and 216-223, are, trypsinlike in all of the enzymes. These structural and kinetic data, confirm that BPTI induces an active conformation in the trypsin(ogen), variants. Thus, changes in BPTI affinity monitor changes in the energetic, cost of inducing a trypsinlike conformation. Although the S1 site and, oxyanion hole are similar in all four variants, the N-terminal and, autolysis loop (residues 142-152) segments have different interactions for, each variant. These results indicate that zymogen activity is controlled, by a simple conformational equilibrium between active and inactive, conformations, and that the autolysis loop and N-terminal segments control, this equilibrium. Together, these data illustrate that induced fit does, not generally contribute to enzyme specificity.
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<StructureSection load='1fy8' size='340' side='right'caption='[[1fy8]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1fy8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FY8 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]] 1.7&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1fy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fy8 OCA], [https://pdbe.org/1fy8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fy8 RCSB], [https://www.ebi.ac.uk/pdbsum/1fy8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fy8 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TRY2_RAT TRY2_RAT]
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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/fy/1fy8_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=1fy8 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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1FY8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus] with CA and SO4 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=1FY8 OCA].
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*[[BPTI 3D structures|BPTI 3D structures]]
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*[[Trypsin 3D structures|Trypsin 3D structures]]
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==Reference==
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__TOC__
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The energetic cost of induced fit catalysis: Crystal structures of trypsinogen mutants with enhanced activity and inhibitor affinity., Pasternak A, White A, Jeffery CJ, Medina N, Cahoon M, Ringe D, Hedstrom L, Protein Sci. 2001 Jul;10(7):1331-42. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11420435 11420435]
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</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
[[Category: Rattus rattus]]
[[Category: Rattus rattus]]
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[[Category: Trypsin]]
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[[Category: Hedstrom L]]
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[[Category: Hedstrom, L.]]
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[[Category: Jeffery CJ]]
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[[Category: Jeffery, C.J.]]
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[[Category: Pasternak A]]
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[[Category: Pasternak, A.]]
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[[Category: Ringe D]]
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[[Category: Ringe, D.]]
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[[Category: White A]]
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[[Category: White, A.]]
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[[Category: CA]]
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[[Category: SO4]]
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[[Category: beta barrel]]
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[[Category: protease-inhibitor complex]]
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[[Category: protein-protein complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:27:42 2007''
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Current revision

CRYSTAL STRUCTURE OF THE DELTAILE16VAL17 RAT ANIONIC TRYPSINOGEN-BPTI COMPLEX

PDB ID 1fy8

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