3lun

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{{Seed}}
 
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[[Image:3lun.jpg|left|200px]]
 
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==Structure of ulilysin mutant M290C==
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The line below this paragraph, containing "STRUCTURE_3lun", creates the "Structure Box" on the page.
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<StructureSection load='3lun' size='340' side='right'caption='[[3lun]], [[Resolution|resolution]] 1.80&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'>[[3lun]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_acetivorans Methanosarcina acetivorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LUN 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]] 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=ARG:ARGININE'>ARG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=VAL:VALINE'>VAL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_3lun| PDB=3lun | 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=3lun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lun OCA], [https://pdbe.org/3lun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lun RCSB], [https://www.ebi.ac.uk/pdbsum/3lun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lun ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ULIL_METAC ULIL_METAC] Metalloprotease which in vitro specifically cleaves IGFBP-2 to -6, insulin, and extracellular matrix proteins but not IGFBP-1 or IGF-II. Shows a preference for substrates with an arginine in the P1' position, the first position downstream of the scissile bond.<ref>PMID:16627477</ref>
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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/lu/3lun_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3lun ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The metzincins are a clan of metallopeptidases consisting of families that share a series of structural elements. Among them is the Met-turn, a tight 1,4-turn found directly below the zinc-binding site, which is structurally and spatially conserved and invariantly shows a methionine at position 3 in all metzincins identified. The reason for this conservation has been a matter of debate since its discovery. We have studied this structural element in Methanosarcina acetivorans ulilysin, the structural prototype of the pappalysin family, by generating 10 mutants that replaced methionine with proteogenic amino acids. We compared recombinant overexpression yields, autolytic and tryptic activation, proteolytic activity, thermal stability, and three-dimensional structure with those of the wild type. All forms were soluble and could be purified, although with varying yields, and three variants underwent autolysis, could be activated by trypsin, and displayed significant proteolytic activity. All variants were analyzed for the thermal stability of their zymogens. None of the mutants analyzed proved more stable or active than the wild type. Both bulky and small side chains, as well as hydrophilic ones, showed diminished thermal stability. Two mutants, leucine and cysteine, crystallized and showed three-dimensional structures that were indistinguishable from the wild type. These studies reveal that the Met-turn acts as a plug that snugly inserts laterally into a core structure created by the protein segment engaged in zinc binding and thus contributes to its structural integrity, which is indispensable for function. Replacement of the methionine with residues that deviate in size, side-chain conformation, and chemical properties impairs the plug-core interaction and prejudices molecular stability and activity.
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===Structure of ulilysin mutant M290C===
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On the relevance of the Met-turn methionine in metzincins.,Tallant C, Garcia-Castellanos R, Baumann U, Gomis-Ruth FX J Biol Chem. 2010 Apr 30;285(18):13951-7. Epub 2010 Mar 4. PMID:20202937<ref>PMID:20202937</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==About this Structure==
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</div>
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3LUN is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Methanosarcina_acetivorans Methanosarcina acetivorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LUN OCA].
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<div class="pdbe-citations 3lun" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Methanosarcina acetivorans]]
[[Category: Methanosarcina acetivorans]]
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[[Category: Baumann, U.]]
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[[Category: Baumann U]]
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[[Category: Garcia-Castellanos, R.]]
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[[Category: Garcia-Castellanos R]]
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[[Category: Gomis-Ruth, F X.]]
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[[Category: Gomis-Ruth FX]]
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[[Category: Tallant, C.]]
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[[Category: Tallant C]]
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[[Category: Calcium]]
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[[Category: Calcium ion binding]]
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[[Category: Disulfide bond]]
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[[Category: Hydrolase]]
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[[Category: Metal ion binding]]
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[[Category: Metal-binding]]
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[[Category: Metallopeptidase]]
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[[Category: Metalloprotease]]
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[[Category: Protease]]
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[[Category: Zinc]]
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[[Category: Zymogen]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 3 17:30:57 2010''
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Current revision

Structure of ulilysin mutant M290C

PDB ID 3lun

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