1esp

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[[Image:1esp.jpg|left|200px]]
 
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==NEUTRAL PROTEASE MUTANT E144S==
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The line below this paragraph, containing "STRUCTURE_1esp", creates the "Structure Box" on the page.
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<StructureSection load='1esp' size='340' side='right'caption='[[1esp]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1esp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ESP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ESP 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]] 2.8&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1esp| PDB=1esp | SCENE= }}
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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=1esp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1esp OCA], [https://pdbe.org/1esp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1esp RCSB], [https://www.ebi.ac.uk/pdbsum/1esp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1esp ProSAT]</span></td></tr>
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</table>
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'''NEUTRAL PROTEASE MUTANT E144S'''
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== Function ==
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[https://www.uniprot.org/uniprot/NPRE_BACCE NPRE_BACCE] Extracellular zinc metalloprotease.
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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The X-ray crystal structure of the Bacillus cereus neutral protease (CNP) active-site mutant E144S, in which the putative general base proposed for the thermolysin-like zinc neutral proteases, Glu144, has been replaced by serine, has been determined to a resolution of 2.8 A. This represents the first crystal structure of an active-site mutant of a zinc neutral protease. The E 144S mutant was crystallized in the hexagonal space group, P6(5)22, with unit-cell dimensions a = b = 76.57, c = 201.91 A. Although the ligands involved in zinc coordination in the active site are identical to those found in the wild-type protein, the mutation results in a modified environment around the zinc ion; particularly with respect to the water molecules. While the structure of the mutant is similar to that of wild type, its protease activity is reduced to 0.16% that of the wild-type CNP and the protein is virtually resistant to autolysis in the presence of calcium. The lowered protease activity of the mutant is consistent with the role proposed for Glu144 as the general base in the catalysis of thermolysin-like neutral proteases [Matthews (1988). Acc. Chem. Res. 21, 333-340]. We suggest that the residual activity of the E144S mutant arises from a water molecule, which is found within hydrogen-bonding distance of Ser144, acting as a general base in the catalytic function of the mutant.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/es/1esp_consurf.spt"</scriptWhenChecked>
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1ESP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ESP OCA].
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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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==Reference==
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</jmolCheckbox>
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E144S active-site mutant of the Bacillus cereus thermolysin-like neutral protease at 2.8 A resolution., Lister SA, Wetmore DR, Roche RS, Codding PW, Acta Crystallogr D Biol Crystallogr. 1996 May 1;52(Pt 3):543-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299677 15299677]
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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=1esp ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Bacillus cereus]]
[[Category: Bacillus cereus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Codding, P W.]]
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[[Category: Codding PW]]
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[[Category: Litster, S A.]]
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[[Category: Litster SA]]
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[[Category: Roche, R S.]]
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[[Category: Roche RS]]
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[[Category: Wetmore, D R.]]
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[[Category: Wetmore DR]]
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[[Category: Inactive mutant e144]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:28:32 2008''
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Current revision

NEUTRAL PROTEASE MUTANT E144S

PDB ID 1esp

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