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1scn

From Proteopedia

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(New page: 200px<br /><applet load="1scn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1scn, resolution 1.9&Aring;" /> '''INACTIVATION OF SUBTI...)
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[[Image:1scn.jpg|left|200px]]<br /><applet load="1scn" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1scn, resolution 1.9&Aring;" />
 
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'''INACTIVATION OF SUBTILISIN CARLSBERG BY N-(TERT-BUTOXYCARBONYL-ALANYL-PROLYL-PHENYLALANYL)-O-BENZOYL HYDROXYLAMINE: FORMATION OF COVALENT ENZYME-INHIBITOR LINKAGE IN THE FORM OF A CARBAMATE DERIVATIVE'''<br />
 
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==Overview==
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==INACTIVATION OF SUBTILISIN CARLSBERG BY N-(TERT-BUTOXYCARBONYL-ALANYL-PROLYL-PHENYLALANYL)-O-BENZOL HYDROXYLAMINE: FORMATION OF COVALENT ENZYME-INHIBITOR LINKAGE IN THE FORM OF A CARBAMATE DERIVATIVE==
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The mechanism of inactivation of serine proteases by, N-peptidyl-O-aroylhydroxylamines was studied by X-ray crystallography., Cocrystals of subtilisin Carlsberg inactivated with, N-((tert-butoxycarbonyl)alanylprolylphenylalanyl)-O-nitrobenzoy, lhydroxylamine were grown, and diffraction data to 1.8-A resolution were, obtained. The resulting electron density maps clearly reveal that the, gamma-oxygen of the catalytic serine forms a carbamate derivative with the, inhibitor. The peptide part of the inhibitor does not form the usual, antiparallel beta-sheet in the P binding cleft but protrudes out of the, active site and is stabilized by a network of water molecules. These, results, combined with kinetic characterization reported previously, [Demuth, H.-U., Schoenlein, C., &amp; Barth, A. (1989b) Biochim. Biophys. Acta, 996, 19-22; Schmidt, C., Schmidt, R., &amp; Demuth, H.-U. (1990) Peptides, (Giralt, E., &amp; Andreu, D., Eds.) ESCOM Science Publishers B.V., Amsterdam], support the existence of at least one intermediate between the formation, of the Michaelis complex and the final product. We suggest a mechanism for, the inactivation of subtilisin Carlsberg by, N-((tert-butoxycarbonyl)alanylprolylphenylalanyl)-O-benzoylhydr oxylamine, whereby a negatively charged Michaelis complex undergoes a Lossen, rearrangement giving rise to an isocyanate intermediate that reacts with, the side chain of the active site serine.
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<StructureSection load='1scn' size='340' side='right'caption='[[1scn]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1scn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SCN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SCN 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]] 1.9&#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=0EF:N-(TERT-BUTOXYCARBONYL)-L-ALANYL-N-[(1R)-1-(CARBOXYAMINO)-2-PHENYLETHYL]-L-PROLINAMIDE'>0EF</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=1scn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1scn OCA], [https://pdbe.org/1scn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1scn RCSB], [https://www.ebi.ac.uk/pdbsum/1scn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1scn ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SUBC_BACLI SUBC_BACLI] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides (Ref.4, PubMed:11109488). Shows high specificity for aromatic and hydrophobic amino acids in the P1 substrate position (PubMed:11109488). May play an important role in the degradation of feather keratin (PubMed:11109488).<ref>PMID:11109488</ref> <ref>PMID:4967581</ref>
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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/sc/1scn_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=1scn 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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1SCN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with CA and NA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SCN OCA].
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*[[Subtilisin 3D structures|Subtilisin 3D structures]]
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== References ==
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==Reference==
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<references/>
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Inactivation of subtilisin Carlsberg by N-((tert-butoxycarbonyl)alanylprolylphenylalanyl)-O-benzoylhydroxyl- amine: formation of a covalent enzyme-inhibitor linkage in the form of a carbamate derivative., Steinmetz AC, Demuth HU, Ringe D, Biochemistry. 1994 Aug 30;33(34):10535-44. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8068694 8068694]
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__TOC__
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[[Category: Single protein]]
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</StructureSection>
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[[Category: Subtilisin]]
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[[Category: Bacillus licheniformis]]
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[[Category: Demuth, H.U.]]
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[[Category: Large Structures]]
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[[Category: Ringe, D.]]
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[[Category: Demuth H-U]]
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[[Category: Steinmetz, A.C.U.]]
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[[Category: Ringe D]]
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[[Category: CA]]
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[[Category: Steinmetz ACU]]
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[[Category: NA]]
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[[Category: complex(serine proteinase/inhibitor)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:16:40 2007''
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Current revision

INACTIVATION OF SUBTILISIN CARLSBERG BY N-(TERT-BUTOXYCARBONYL-ALANYL-PROLYL-PHENYLALANYL)-O-BENZOL HYDROXYLAMINE: FORMATION OF COVALENT ENZYME-INHIBITOR LINKAGE IN THE FORM OF A CARBAMATE DERIVATIVE

PDB ID 1scn

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