1cse

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(New page: 200px<br /><applet load="1cse" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cse, resolution 1.2&Aring;" /> '''THE HIGH-RESOLUTION X...)
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[[Image:1cse.gif|left|200px]]<br /><applet load="1cse" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cse, resolution 1.2&Aring;" />
 
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'''THE HIGH-RESOLUTION X-RAY CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN SUBTILISIN CARLSBERG AND EGLIN C, AN ELASTASE INHIBITOR FROM THE LEECH HIRUDO MEDICINALIS. STRUCTURAL ANALYSIS, SUBTILISIN STRUCTURE AND INTERFACE GEOMETRY'''<br />
 
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==Overview==
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==THE HIGH-RESOLUTION X-RAY CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN SUBTILISIN CARLSBERG AND EGLIN C, AN ELASTASE INHIBITOR FROM THE LEECH HIRUDO MEDICINALIS. STRUCTURAL ANALYSIS, SUBTILISIN STRUCTURE AND INTERFACE GEOMETRY==
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Triclinic crystals of the complex formed by eglin with subtilisin, Carlsberg were analyzed by X-ray diffraction. The crystal and molecular, structure of this complex was determined with data that extended to, 0.12-nm resolution by a combination of Patterson search methods and, isomorphous replacement techniques. Its structure was refined to a, crystallographic R value of 0.178 (1.0-0.12 nm) using an energy-restraint, least-squares procedure. The complete subtilisin molecule could be traced, without ambiguity in the refined electron density. The eglin component, from which an amino-terminal segment is cleaved off, is only defined from, Lys8I (i.e. the lysine residue 8 of the inhibitor) onwards. Per unit cell, 436 fixed solvent molecules and 2 calcium ions were located. In spite of, 84 amino acid replacements and one deletion, subtilisin Carlsberg exhibits, a very similar polypeptide fold to subtilisin BPN'. The root-mean-square, deviations of all alpha-carbon atoms (excluding those at the deletion, site) from models of subtilisin BPN' [Alden, R. A., Birktoft, J. J., Kraut, J., Robertus, J. D. &amp; Wright, C. S. (1971) Biochem. Biophys. Res., Commun. 45, 337-344] and subtilisin Novo [Drenth, J., Hol, W. G. J., Jansonius, J. N. &amp; Kockoek, R. (1972) Eur. J. Biochem. 25, 177-181] are, 0.077 nm and 0.103 nm. Most of these deviations result from global shifts, rather than changes of the local geometry. The single-residue deletion at, position 56 affects only the surrounding conformation. Two sites of high, electron density and close distances to surrounding oxygen ligands have, been found in the Carlsberg enzyme which are probably occupied by calcium, ions. Eglin consists of a twisted four-stranded beta-sheet flanked by an, alpha-helix and by an exposed proteinase binding loop on opposite sides., Around the reactive site, Leu45I-Asp46I, this loop is mainly stabilized by, electrostatic/hydrogen bond interactions with the side chains of two, arginine residues which project from the hydrophobic core [Bode, W., Papamokos, E., Musil, D., Seemuller, W. &amp; Fritz, H. (1986) EMBO J. 5, 813-818]. The reactive site loop conformation resembles that found in, other 'small' proteinase inhibitors. The scissile peptide bond is not, cleaved but its carbonyl group is slightly distorted from planar geometry., Most of the intermolecular contacts are contributed by the nine residues, of the reactive-site loop Gly40I-Arg48I.(ABSTRACT TRUNCATED AT 400 WORDS)
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<StructureSection load='1cse' size='340' side='right'caption='[[1cse]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1cse]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] and [https://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CSE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CSE 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]] 1.2&#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></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=1cse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cse OCA], [https://pdbe.org/1cse PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cse RCSB], [https://www.ebi.ac.uk/pdbsum/1cse PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cse ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/B0FXJ2_BACIU B0FXJ2_BACIU]
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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/cs/1cse_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=1cse 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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1CSE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] and [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1CSE OCA].
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*[[Eglin|Eglin]]
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*[[Subtilisin 3D structures|Subtilisin 3D structures]]
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==Reference==
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__TOC__
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The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis. Structural analysis, subtilisin structure and interface geometry., Bode W, Papamokos E, Musil D, Eur J Biochem. 1987 Aug 3;166(3):673-92. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=3301348 3301348]
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</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Hirudo medicinalis]]
[[Category: Hirudo medicinalis]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Subtilisin]]
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[[Category: Bode W]]
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[[Category: Bode, W.]]
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[[Category: CA]]
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[[Category: complex(serine proteinase-inhibitor)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:43:17 2007''
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Current revision

THE HIGH-RESOLUTION X-RAY CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN SUBTILISIN CARLSBERG AND EGLIN C, AN ELASTASE INHIBITOR FROM THE LEECH HIRUDO MEDICINALIS. STRUCTURAL ANALYSIS, SUBTILISIN STRUCTURE AND INTERFACE GEOMETRY

PDB ID 1cse

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