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1sgc

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[[Image:1sgc.gif|left|200px]]<br /><applet load="1sgc" size="350" color="white" frame="true" align="right" caption="1sgc, resolution 1.8&Aring;" />
 
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'''THE 1.8 ANGSTROMS STRUCTURE OF THE COMPLEX BETWEEN CHYMOSTATIN AND STREPTOMYCES GRISEUS PROTEASE A. A MODEL FOR SERINE PROTEASE CATALYTIC TETRAHEDRAL INTERMEDIATES'''<br />
 
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==Overview==
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==THE 1.8 ANGSTROMS STRUCTURE OF THE COMPLEX BETWEEN CHYMOSTATIN AND STREPTOMYCES GRISEUS PROTEASE A. A MODEL FOR SERINE PROTEASE CATALYTIC TETRAHEDRAL INTERMEDIATES==
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The naturally occurring serine protease inhibitor, chymostatin, forms a hemiacetal adduct with the catalytic Ser195 residue of Streptomyces griseus protease A. Restrained parameter least-squares refinement of this complex to 1.8 A resolution has produced an R index of 0 X 123 for the 11,755 observed reflections. The refined distance of the carbonyl carbon atom of the aldehyde to O gamma of Ser195 is 1 X 62 A. Both the R and S configurations of the hemiacetal occur in equal populations, with the end result resembling the expected configuration for a covalent tetrahedral product intermediate of a true substrate. This study strengthens the concept that serine proteases stabilize a covalent, tetrahedrally co-ordinated species and elaborates those features of the enzyme responsible for this effect. We propose that a major driving force for the hydrolysis of peptide bonds by serine proteases is the non-planar distortion of the scissile bond by the enzyme, which thereby lowers the activation energy barrier to hydrolysis by eliminating the resonance stabilization energy of the peptide bond.
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<StructureSection load='1sgc' size='340' side='right'caption='[[1sgc]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1sgc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_griseus Streptomyces griseus] and [https://en.wikipedia.org/wiki/Streptomyces_hygroscopicus Streptomyces hygroscopicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SGC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SGC 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]] 1.8&#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=CSI:AMINO-(2-IMINO-HEXAHYDRO-PYRIMIDIN-4-YL)-ACETIC+ACID'>CSI</scene>, <scene name='pdbligand=PHA:PHENYLALANINAL'>PHA</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=1sgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sgc OCA], [https://pdbe.org/1sgc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sgc RCSB], [https://www.ebi.ac.uk/pdbsum/1sgc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sgc ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PRTA_STRGR PRTA_STRGR] Has a primary specificity for large aliphatic or aromatic amino acids.
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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/sg/1sgc_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=1sgc 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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1SGC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_griseus Streptomyces griseus] with <scene name='pdbligand=CST:'>CST</scene> as [[ligand]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SGC OCA].
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*[[Proteinase 3D structures|Proteinase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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The 1.8 A structure of the complex between chymostatin and Streptomyces griseus protease A. A model for serine protease catalytic tetrahedral intermediates., Delbaere LT, Brayer GD, J Mol Biol. 1985 May 5;183(1):89-103. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/3892018 3892018]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Streptomyces griseus]]
[[Category: Streptomyces griseus]]
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[[Category: Brayer, G D.]]
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[[Category: Streptomyces hygroscopicus]]
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[[Category: Delbaere, L T.J.]]
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[[Category: Brayer GD]]
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[[Category: CST]]
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[[Category: Delbaere LTJ]]
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[[Category: hydrolase (serine proteinase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Mar 18 20:00:42 2008''
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Current revision

THE 1.8 ANGSTROMS STRUCTURE OF THE COMPLEX BETWEEN CHYMOSTATIN AND STREPTOMYCES GRISEUS PROTEASE A. A MODEL FOR SERINE PROTEASE CATALYTIC TETRAHEDRAL INTERMEDIATES

PDB ID 1sgc

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