3l6w
From Proteopedia
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| - | + | ==Structure of the collar functional unit (KLH1-H) of keyhole limpet hemocyanin== | |
| - | + | <StructureSection load='3l6w' size='340' side='right' caption='[[3l6w]], [[Resolution|resolution]] 4.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L6W FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3eu2|3eu2]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3l6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l6w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3l6w RCSB], [http://www.ebi.ac.uk/pdbsum/3l6w PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == 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/chain_selection.php?pdb_ID=2ata 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. | ||
| - | + | 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> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Megathura crenulata]] | [[Category: Megathura crenulata]] | ||
| - | [[Category: Barends, T R.M | + | [[Category: Barends, T R.M]] |
| - | [[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: Copper-binding protein]] | ||
[[Category: Cupredoxin domain]] | [[Category: Cupredoxin domain]] | ||
Revision as of 15:32, 18 December 2014
Structure of the collar functional unit (KLH1-H) of keyhole limpet hemocyanin
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