1oxy: Difference between revisions

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{{Seed}}
[[Image:1oxy.png|left|200px]]


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==CRYSTALLOGRAPHIC ANALYSIS OF OXYGENATED AND DEOXYGENATED STATES OF ARTHROPOD HEMOCYANIN SHOWS UNUSUAL DIFFERENCES==
The line below this paragraph, containing "STRUCTURE_1oxy", creates the "Structure Box" on the page.
<StructureSection load='1oxy' size='340' side='right'caption='[[1oxy]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1oxy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Limulus_polyphemus Limulus polyphemus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OXY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OXY FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#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=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr>
{{STRUCTURE_1oxy|  PDB=1oxy  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oxy OCA], [https://pdbe.org/1oxy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oxy RCSB], [https://www.ebi.ac.uk/pdbsum/1oxy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oxy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HCY2_LIMPO HCY2_LIMPO] Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.
== 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/ox/1oxy_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=1oxy ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The X-ray structure of an oxygenated hemocyanin molecule, subunit II of Limulus polyphemus hemocyanin, was determined at 2.4 A resolution and refined to a crystallographic R-factor of 17.1%. The 73-kDa subunit crystallizes with the symmetry of the space group R32 with one subunit per asymmetric unit forming hexamers with 32 point group symmetry. Molecular oxygen is bound to a dinuclear copper center in the protein's second domain, symmetrically between and equidistant from the two copper atoms. The copper-copper distance in oxygenated Limulus hemocyanin is 3.6 +/- 0.2 A, which is surprisingly 1 A less than that seen previously in deoxygenated Limulus polyphemus subunit II hemocyanin (Hazes et al., Protein Sci. 2:597, 1993). Away from the oxygen binding sites, the tertiary and quaternary structures of oxygenated and deoxygenated Limulus subunit II hemocyanins are quite similar. A major difference in tertiary structures is seen, however, when the Limulus structures are compared with deoxygenated Panulirus interruptus hemocyanin (Volbeda, A., Hol, W.G.J.J. Mol. Biol. 209:249, 1989) where the position of domain 1 is rotated by 8 degrees with respect to domains 2 and 3. We postulate this rotation plays an important role in cooperativity and regulation of oxygen affinity in all arthropod hemocyanins.


===CRYSTALLOGRAPHIC ANALYSIS OF OXYGENATED AND DEOXYGENATED STATES OF ARTHROPOD HEMOCYANIN SHOWS UNUSUAL DIFFERENCES===
Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences.,Magnus KA, Hazes B, Ton-That H, Bonaventura C, Bonaventura J, Hol WG Proteins. 1994 Aug;19(4):302-9. PMID:7984626<ref>PMID:7984626</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_7984626}}, adds the Publication Abstract to the page
<div class="pdbe-citations 1oxy" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 7984626 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_7984626}}
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</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1OXY is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Limulus_polyphemus Limulus polyphemus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OXY OCA].
 
==Reference==
<ref group="xtra">PMID:7984626</ref><references group="xtra"/>
[[Category: Limulus polyphemus]]
[[Category: Limulus polyphemus]]
[[Category: Magnus, K.]]
[[Category: Magnus K]]
[[Category: Ton-that, H.]]
[[Category: Ton-that H]]
[[Category: Oxygen transport]]
 
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Retrieved from "https://proteopedia.org/1oxy"