5zjk

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Current revision (10:28, 27 March 2024) (edit) (undo)
 
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<StructureSection load='5zjk' size='340' side='right'caption='[[5zjk]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='5zjk' size='340' side='right'caption='[[5zjk]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5zjk]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Myroides_sp._cslb8 Myroides sp. cslb8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZJK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZJK FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5zjk]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Myroides_sp._CSLB8 Myroides sp. CSLB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZJK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZJK FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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]] 2.6&#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=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5zjk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zjk OCA], [https://pdbe.org/5zjk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zjk RCSB], [https://www.ebi.ac.uk/pdbsum/5zjk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zjk ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5zjk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zjk OCA], [https://pdbe.org/5zjk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zjk RCSB], [https://www.ebi.ac.uk/pdbsum/5zjk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zjk ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A0P0DZ84_9FLAO A0A0P0DZ84_9FLAO]
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Myroilysin is a novel bacterial member of M12A metalloproteases family with an uncommon "cysteine switch" activation mechanism and a unique "cap" structure. However, activation of pro-myroilysin is elusive. Here, mature myroilysin was obtained for structure determination by treating pro-myroilysin with trypsin. The structure of mature myroilysin showed that the active-site zinc ion of the mature protein is coordinated by three histidine residues, a water molecule, and a tyrosine residue (Tyr208) in the conserved Met-turn motif (SIMHY). The "cap" structure moves away from the active-site to leave the active cleft open; the newly formed N-terminus is deeply buried in myroilysin, and Glu151 forms a salt bridge directly with the first amino acid residue (Gly38), whereas they are far from each other in the pro-myroilysin. The mutation of Tyr208 indicates that Tyr208 plays an important role in activity of myroilysin. The proteolytic activity and thermostability of mutant E151A decreased dramatically, implying that Glu151 is not only important for catalysis, but also crucial for structural stability in myroilysin. Structural comparison also reveals differences existed between myroilysin and astacin. Our biochemical and structural data provide new insights into the activation of myroilysin and functional involvement of crucial residues Tyr208 and Glu151.
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Crystal structure of mature myroilysin and implication for its activation mechanism.,Ran T, Li W, Sun B, Xu M, Qiu S, Xu DQ, He J, Wang W Int J Biol Macromol. 2019 Nov 28. pii: S0141-8130(19)36556-0. doi:, 10.1016/j.ijbiomac.2019.11.205. PMID:31785296<ref>PMID:31785296</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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</div>
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<div class="pdbe-citations 5zjk" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Myroides sp. cslb8]]
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[[Category: Myroides sp. CSLB8]]
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[[Category: Li, W D]]
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[[Category: Li WD]]
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[[Category: Ran, T T]]
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[[Category: Ran TT]]
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[[Category: Wang, W W]]
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[[Category: Wang WW]]
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[[Category: Xu, D Q]]
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[[Category: Xu DQ]]
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[[Category: Hydrolase]]
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Current revision

Structure of myroilysin

PDB ID 5zjk

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