3l6w

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{{STRUCTURE_3l6w| PDB=3l6w | SCENE= }}
 
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===Structure of the collar functional unit (KLH1-H) of keyhole limpet hemocyanin===
 
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{{ABSTRACT_PUBMED_20025608}}
 
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==About this Structure==
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==Structure of the collar functional unit (KLH1-H) of keyhole limpet hemocyanin==
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[[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].
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<StructureSection load='3l6w' size='340' side='right'caption='[[3l6w]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
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== Structural highlights ==
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<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>
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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]] 4&#8491;</td></tr>
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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=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>
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</table>
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== Function ==
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[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>
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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/l6/3l6w_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=3l6w 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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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.
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==Reference==
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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>
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<ref group="xtra">PMID:020025608</ref><references group="xtra"/><references/>
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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 3l6w" 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: Megathura crenulata]]
[[Category: Megathura crenulata]]
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[[Category: Barends, T R.M.]]
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[[Category: Barends TRM]]
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[[Category: Buechler, K.]]
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[[Category: Buechler K]]
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[[Category: Decker, H.]]
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[[Category: Decker H]]
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[[Category: Jaenicke, E.]]
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[[Category: Jaenicke E]]
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[[Category: Markl, J.]]
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[[Category: Markl J]]
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[[Category: Copper-binding protein]]
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[[Category: Cupredoxin domain]]
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[[Category: Hemocyanin]]
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[[Category: Metal-binding]]
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[[Category: Oxygen binding]]
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Current revision

Structure of the collar functional unit (KLH1-H) of keyhole limpet hemocyanin

PDB ID 3l6w

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