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1oxy

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[[Image:1oxy.gif|left|200px]]
 
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{{Structure
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==CRYSTALLOGRAPHIC ANALYSIS OF OXYGENATED AND DEOXYGENATED STATES OF ARTHROPOD HEMOCYANIN SHOWS UNUSUAL DIFFERENCES==
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|PDB= 1oxy |SIZE=350|CAPTION= <scene name='initialview01'>1oxy</scene>, resolution 2.4&Aring;
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<StructureSection load='1oxy' size='340' side='right'caption='[[1oxy]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>
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<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>
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|ACTIVITY=
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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]] 2.4&#8491;</td></tr>
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|GENE=
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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>
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|DOMAIN=
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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=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>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oxy OCA], [http://www.ebi.ac.uk/pdbsum/1oxy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oxy RCSB]</span>
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== Function ==
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}}
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[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.
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== Evolutionary Conservation ==
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'''CRYSTALLOGRAPHIC ANALYSIS OF OXYGENATED AND DEOXYGENATED STATES OF ARTHROPOD HEMOCYANIN SHOWS UNUSUAL DIFFERENCES'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ox/1oxy_consurf.spt"</scriptWhenChecked>
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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.
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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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==About this Structure==
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</jmolCheckbox>
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1OXY is a [[Single protein]] 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].
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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=1oxy ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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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:[http://www.ncbi.nlm.nih.gov/pubmed/7984626 7984626]
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Limulus polyphemus]]
[[Category: Limulus polyphemus]]
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[[Category: Single protein]]
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[[Category: Magnus K]]
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[[Category: Magnus, K.]]
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[[Category: Ton-that H]]
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[[Category: Ton-that, H.]]
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[[Category: oxygen transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:51:58 2008''
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Current revision

CRYSTALLOGRAPHIC ANALYSIS OF OXYGENATED AND DEOXYGENATED STATES OF ARTHROPOD HEMOCYANIN SHOWS UNUSUAL DIFFERENCES

PDB ID 1oxy

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