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1cis

From Proteopedia

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[[Image:1cis.jpg|left|200px]]<br /><applet load="1cis" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cis" />
 
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'''CONTEXT DEPENDENCE OF PROTEIN SECONDARY STRUCTURE FORMATION. THE THREE-DIMENSIONAL STRUCTURE AND STABILITY OF A HYBRID BETWEEN CHYMOTRYPSIN INHIBITOR 2 AND HELIX E FROM SUBTILISIN CARLSBERG'''<br />
 
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==Overview==
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==CONTEXT DEPENDENCE OF PROTEIN SECONDARY STRUCTURE FORMATION. THE THREE-DIMENSIONAL STRUCTURE AND STABILITY OF A HYBRID BETWEEN CHYMOTRYPSIN INHIBITOR 2 AND HELIX E FROM SUBTILISIN CARLSBERG==
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The loop region of chymotrypsin inhibitor 2 from barley has been employed as a scaffold for testing the intrinsic propensity of a peptide fragment to form a secondary structure. The helix formation of the nine amino acid residue segment Lys-Gln-Ala-Val-Asp-Asn-Ala-Tyr-Ala of helix E from subtilisin Carlsberg has been studied by the construction of a hybrid consisting of chymotrypsin inhibitor 2 (CI2) where part of the active loop has been replaced by the nonapeptide. An expression system for a truncated form of CI2 where the 19 structureless residues of the N-terminus have been removed and Leu20 replaced by methionyl was constructed from the entire 83-residue wild-type CI2 gene by polymerase chain reaction methodology. The gene encoding the hybrid was constructed from the truncated inhibitor gene. The stability of the truncated inhibitor and of the hybrid toward guanidinium chloride denaturation was examined. From these measurements, the energy of unfolding in pure water was extrapolated to 30.5 +/- 1.0 kJ/mol for the truncated inhibitor and 10.9 +/- 0.3 kJ/mol for the hybrid. These energies show that the stability of CI2 is unaffected by the N-terminal truncation but severely decreased by the loop mutations. The three-dimensional structure of the hybrid protein has been determined in solution by nuclear magnetic resonance spectroscopy using 893 distance restraints and 84 torsional angle restraints. The average root-mean-square deviation (rmsd) of 15 structures compared to their geometrical average was 0.8 +/- 0.2 A for heavy backbone atoms and 1.3 +/- 0.2 A for all heavy atoms.(ABSTRACT TRUNCATED AT 250 WORDS)
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<StructureSection load='1cis' size='340' side='right'caption='[[1cis]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1cis]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis] and [https://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CIS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CIS 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">Solution NMR</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=1cis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cis OCA], [https://pdbe.org/1cis PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cis RCSB], [https://www.ebi.ac.uk/pdbsum/1cis PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cis ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ICI2_HORVU ICI2_HORVU] Inhibits both subtilisin and chymotrypsin.
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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/ci/1cis_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=1cis 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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1CIS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CIS OCA].
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*[[Chymotrypsin inhibitor 3D structures|Chymotrypsin inhibitor 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Context dependence of protein secondary structure formation: the three-dimensional structure and stability of a hybrid between chymotrypsin inhibitor 2 and helix E from subtilisin Carlsberg., Osmark P, Sorensen P, Poulsen FM, Biochemistry. 1993 Oct 19;32(41):11007-14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8218165 8218165]
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[[Category: Bacillus licheniformis]]
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[[Category: Single protein]]
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[[Category: Hordeum vulgare]]
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[[Category: Osmark, P.]]
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[[Category: Large Structures]]
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[[Category: Poulsen, F M.]]
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[[Category: Osmark P]]
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[[Category: Sorensen, P.]]
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[[Category: Poulsen FM]]
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[[Category: hybrid protein]]
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[[Category: Sorensen P]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:34 2008''
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Current revision

CONTEXT DEPENDENCE OF PROTEIN SECONDARY STRUCTURE FORMATION. THE THREE-DIMENSIONAL STRUCTURE AND STABILITY OF A HYBRID BETWEEN CHYMOTRYPSIN INHIBITOR 2 AND HELIX E FROM SUBTILISIN CARLSBERG

PDB ID 1cis

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