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{{STRUCTURE_3l6w|  PDB=3l6w  |  SCENE=  }}
===Structure of the collar functional unit (KLH1-H) of keyhole limpet hemocyanin===
{{ABSTRACT_PUBMED_20025608}}


==About this Structure==
==Structure of the collar functional unit (KLH1-H) of keyhole limpet hemocyanin==
[[3l6w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Megathura_crenulata Megathura crenulata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L6W OCA].  
<StructureSection load='3l6w' size='340' side='right'caption='[[3l6w]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3l6w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Megathura_crenulata Megathura crenulata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L6W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L6W FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4&#8491;</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=3l6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l6w OCA], [https://pdbe.org/3l6w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l6w RCSB], [https://www.ebi.ac.uk/pdbsum/3l6w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l6w ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HCY1_MEGCR HCY1_MEGCR] Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.<ref>PMID:8829804</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l6/3l6w_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=3l6w ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Haemocyanins are multimeric oxygen transport proteins, which bind oxygen to type 3 copper sites. Arthropod haemocyanins contain 75-kDa subunits, whereas molluscan haemocyanins contain 350-400-kDa subunits comprising seven or eight different 50 kDa FUs (functional units) designated FU-a to FU-h, each with an active site. FU-h possesses a tail of 100 amino acids not present in the other FUs. In the present study we show by X-ray crystallography that in FU-h of KLH1 (keyhole-limpet-haemocyanin isoform 1) the structure of the tail domain is cupredoxin-like but contains no copper. The copper-free domain 3 in arthropod haemocyanin subunits has also recently been reinterpreted as being cupredoxin-like. We propose that the cupredoxin-like domain in both haemocyanin types once served to upload copper to the active site of the oxygen-binding domain.


==Reference==
Cupredoxin-like domains in haemocyanins.,Jaenicke E, Buchler K, Markl J, Decker H, Barends TR Biochem J. 2010 Feb 24;426(3):373-8. PMID:20025608<ref>PMID:20025608</ref>
<ref group="xtra">PMID:020025608</ref><references group="xtra"/><references/>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3l6w" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Megathura crenulata]]
[[Category: Megathura crenulata]]
[[Category: Barends, T R.M.]]
[[Category: Barends TRM]]
[[Category: Buechler, K.]]
[[Category: Buechler K]]
[[Category: Decker, H.]]
[[Category: Decker H]]
[[Category: Jaenicke, E.]]
[[Category: Jaenicke E]]
[[Category: Markl, J.]]
[[Category: Markl J]]
[[Category: Copper-binding protein]]
[[Category: Cupredoxin domain]]
[[Category: Hemocyanin]]
[[Category: Metal-binding]]
[[Category: Oxygen binding]]
Retrieved from "https://proteopedia.org/3l6w"