3ixw
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ixw]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Androctonus_australis Androctonus australis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IXW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IXW FirstGlance]. <br> | <table><tr><td colspan='2'>[[3ixw]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Androctonus_australis Androctonus australis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IXW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IXW FirstGlance]. <br> | ||
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 8Å</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=3ixw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ixw OCA], [https://pdbe.org/3ixw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ixw RCSB], [https://www.ebi.ac.uk/pdbsum/3ixw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ixw 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=3ixw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ixw OCA], [https://pdbe.org/3ixw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ixw RCSB], [https://www.ebi.ac.uk/pdbsum/3ixw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ixw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/HCY6_ANDAU HCY6_ANDAU] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=3ixw ConSurf]. | </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=3ixw ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Phenoloxidases (POs) occur in all organisms and are involved in skin and hair coloring in mammals, and initiating melanization in wound healing. Mutation or overexpression of PO can cause albinism or melanoma, respectively. SDS can convert inactive PO and the oxygen carrier hemocyanin (Hc) into enzymatically active PO. Here we present single-particle cryo-EM maps at subnanometer resolution and pseudoatomic models of the 24-oligomeric Hc from scorpion Pandinus imperator in resting and SDS-activated states. Our structural analyses led to a plausible mechanism of Hc enzyme PO activation: upon SDS activation, the intrinsically flexible Hc domain I twists away from domains II and III in each subunit, exposing the entrance to the active site; this movement is stabilized by enhanced interhexamer and interdodecamer interactions, particularly in the central linker subunits. This mechanism could be applicable to other type 3 copper proteins, as the active site is highly conserved. | ||
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- | Structural mechanism of SDS-induced enzyme activity of scorpion hemocyanin revealed by electron cryomicroscopy.,Cong Y, Zhang Q, Woolford D, Schweikardt T, Khant H, Dougherty M, Ludtke SJ, Chiu W, Decker H Structure. 2009 May 13;17(5):749-58. PMID:19446530<ref>PMID:19446530</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 3ixw" style="background-color:#fffaf0;"></div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</SX> | </SX> | ||
[[Category: Androctonus australis]] | [[Category: Androctonus australis]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Chiu | + | [[Category: Chiu W]] |
- | [[Category: Cong | + | [[Category: Cong Y]] |
- | [[Category: Decker | + | [[Category: Decker H]] |
- | [[Category: Khant | + | [[Category: Khant H]] |
- | [[Category: Ludtke | + | [[Category: Ludtke S]] |
- | [[Category: Schweikardt | + | [[Category: Schweikardt T]] |
- | [[Category: Woolford | + | [[Category: Woolford D]] |
- | [[Category: Zhang | + | [[Category: Zhang Q]] |
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Current revision
Scorpion Hemocyanin activated state pseudo atomic model built based on cryo-EM density map
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Categories: Androctonus australis | Large Structures | Chiu W | Cong Y | Decker H | Khant H | Ludtke S | Schweikardt T | Woolford D | Zhang Q