1zvj

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[[Image:1zvj.gif|left|200px]]
 
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==Structure of Kumamolisin-AS mutant, D164N==
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The line below this paragraph, containing "STRUCTURE_1zvj", creates the "Structure Box" on the page.
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<StructureSection load='1zvj' size='340' side='right'caption='[[1zvj]], [[Resolution|resolution]] 2.03&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'>[[1zvj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alicyclobacillus_sendaiensis Alicyclobacillus sendaiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZVJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZVJ FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.03&#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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1zvj| PDB=1zvj | 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=1zvj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zvj OCA], [https://pdbe.org/1zvj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zvj RCSB], [https://www.ebi.ac.uk/pdbsum/1zvj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zvj ProSAT]</span></td></tr>
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</table>
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'''Structure of Kumamolisin-AS mutant, D164N'''
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== Function ==
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[https://www.uniprot.org/uniprot/Q8GB88_9BACL Q8GB88_9BACL]
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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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Kumamolisin-As is an acid collagenase with a subtilisin-like fold. Its active site contains a unique catalytic triad, Ser278-Glu78-Asp82, and a putative transition-state stabilizing residue, Asp164. In this study, the mutants D164N and E78H/D164N were engineered in order to replace parts of the catalytic machinery of kumamolisin-As with the residues found in the equivalent positions in subtilisin. Unlike the wild-type and D164N proenzymes, which undergo instantaneous processing to produce their 37-kDa mature forms, the expressed E78H/D164N proenzyme exists as an equilibrated mixture of the nicked and intact forms of the precursor. X-ray crystallographic structures of the mature forms of the two mutants showed that, in each of them, the catalytic Ser278 makes direct hydrogen bonds with the side chain of Asn164. In addition, His78 of the double mutant is distant from Ser278 and Asp82, and the catalytic triad no longer exists. Consistent with these structural alterations around the active site, these mutants showed only low catalytic activity (relative k(cat) at pH 4.0 1.3% for D164N and 0.0001% for E78H/D164N). pH-dependent kinetic studies showed that the single D164N substitution did not significantly alter the logk(cat) vs. pH and log(k(cat)/Km) vs. pH profiles of the enzyme. In contrast, the double mutation resulted in a dramatic switch of the logk(cat) vs. pH profile to one that was consistent with catalysis by means of the Ser278-His78 dyad and Asn164, which may also account for the observed ligation/cleavage equilibrium of the precursor of E78H/D164N. These results corroborate the mechanistic importance of the glutamate-mediated catalytic triad and oxyanion-stabilizing aspartic acid residue for low-pH peptidase activity of the enzyme.
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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/zv/1zvj_consurf.spt"</scriptWhenChecked>
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1ZVJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Alicyclobacillus_sendaiensis Alicyclobacillus sendaiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZVJ 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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Processing, catalytic activity and crystal structures of kumamolisin-As with an engineered active site., Okubo A, Li M, Ashida M, Oyama H, Gustchina A, Oda K, Dunn BM, Wlodawer A, Nakayama T, FEBS J. 2006 Jun;273(11):2563-76. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16704427 16704427]
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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=1zvj ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Alicyclobacillus sendaiensis]]
[[Category: Alicyclobacillus sendaiensis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Gustchina, A.]]
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[[Category: Gustchina A]]
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[[Category: Li, M.]]
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[[Category: Li M]]
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[[Category: Nakayama, T.]]
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[[Category: Nakayama T]]
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[[Category: Wlodawer, A.]]
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[[Category: Wlodawer A]]
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[[Category: D164n]]
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[[Category: Kumamolisin-a]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:07:41 2008''
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Current revision

Structure of Kumamolisin-AS mutant, D164N

PDB ID 1zvj

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