1siu

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(New page: 200px<br /><applet load="1siu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1siu, resolution 2.31&Aring;" /> '''KUMAMOLISIN-AS E78H ...)
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[[Image:1siu.jpg|left|200px]]<br /><applet load="1siu" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1siu, resolution 2.31&Aring;" />
 
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'''KUMAMOLISIN-AS E78H MUTANT'''<br />
 
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==Overview==
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==KUMAMOLISIN-AS E78H MUTANT==
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Kumamolisin-As (previously called ScpA) is the first known example of a, collagenase from the sedolisin family (MEROPS S53). This enzyme is active, at low pH and in elevated temperatures. In this study that used x-ray, crystallographic and biochemical methods, we investigated the structural, basis of the preference of this enzyme for collagen and the importance of, a glutamate residue in the unique catalytic triad, (Ser(278)-Glu(78)-Asp(82)) for enzymatic activity. Crystal structures of, the uninhibited enzyme and its complex with a covalently bound inhibitor, N-acetyl-isoleucyl-prolyl-phenylalaninal, showed the occurrence of a, narrow S2 pocket and a groove that encompasses the active site and is rich, in negative charges. Limited endoproteolysis studies of bovine type-I, collagen as well as kinetic studies using peptide libraries randomized at, P1 and P1', showed very strong preference for arginine at the P1 position, which correlated very well with the presence of a negatively charged, residue in the S1 pocket of the enzyme. All of these features, together, with those predicted through comparisons with fiddler crab collagenase, a, serine peptidase, rationalize the enzyme's preference for collagen. A, comparison of the Arrhenius plots of the activities of kumamolisin-As with, either collagen or peptides as substrates suggests that collagen should be, relaxed before proteolysis can occur. The E78H mutant, in which the, catalytic triad was engineered to resemble that of subtilisin, showed only, 0.01% activity of the wild-type enzyme, and its structure revealed that, Ser(278), His(78), and Asp(82) do not interact with each other; thus, the, canonical catalytic triad is disrupted.
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<StructureSection load='1siu' size='340' side='right'caption='[[1siu]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1siu]] 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=1SIU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SIU FirstGlance]. <br>
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1SIU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Alicyclobacillus_sendaiensis Alicyclobacillus sendaiensis] with SO4 and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SIU OCA].
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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]] 2.31&#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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==Reference==
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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=1siu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1siu OCA], [https://pdbe.org/1siu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1siu RCSB], [https://www.ebi.ac.uk/pdbsum/1siu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1siu ProSAT]</span></td></tr>
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Crystallographic and biochemical investigations of kumamolisin-As, a serine-carboxyl peptidase with collagenase activity., Wlodawer A, Li M, Gustchina A, Tsuruoka N, Ashida M, Minakata H, Oyama H, Oda K, Nishino T, Nakayama T, J Biol Chem. 2004 May 14;279(20):21500-10. Epub 2004 Mar 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15014068 15014068]
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</table>
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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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[[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/si/1siu_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=1siu 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: Ashida, M.]]
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[[Category: Ashida M]]
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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: Minakata, H.]]
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[[Category: Minakata H]]
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[[Category: Nakayama, T.]]
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[[Category: Nakayama T]]
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[[Category: Nishino, T.]]
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[[Category: Nishino T]]
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[[Category: Oda, K.]]
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[[Category: Oda K]]
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[[Category: Oyama, H.]]
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[[Category: Oyama H]]
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[[Category: Tsuruoka, N.]]
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[[Category: Tsuruoka N]]
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[[Category: Wlodawer, A.]]
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[[Category: Wlodawer A]]
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[[Category: CA]]
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[[Category: SO4]]
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[[Category: e78h]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:35:40 2007''
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Current revision

KUMAMOLISIN-AS E78H MUTANT

PDB ID 1siu

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