1js8

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[[Image:1js8.gif|left|200px]]
[[Image:1js8.gif|left|200px]]
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{{Structure
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|PDB= 1js8 |SIZE=350|CAPTION= <scene name='initialview01'>1js8</scene>, resolution 2.3&Aring;
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The line below this paragraph, containing "STRUCTURE_1js8", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CUO:CU2-O2+CLUSTER'>CUO</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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{{STRUCTURE_1js8| PDB=1js8 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1js8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1js8 OCA], [http://www.ebi.ac.uk/pdbsum/1js8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1js8 RCSB]</span>
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'''Structure of a Functional Unit from Octopus Hemocyanin'''
'''Structure of a Functional Unit from Octopus Hemocyanin'''
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[[Category: Holde, K E.van.]]
[[Category: Holde, K E.van.]]
[[Category: Miller, K I.]]
[[Category: Miller, K I.]]
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[[Category: copper]]
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[[Category: Copper]]
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[[Category: glycoprotein]]
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[[Category: Glycoprotein]]
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[[Category: mollusc]]
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[[Category: Mollusc]]
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[[Category: oxygen-transport]]
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[[Category: Oxygen-transport]]
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[[Category: thioether bond]]
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[[Category: Thioether bond]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:49:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:38:15 2008''
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Revision as of 18:49, 2 May 2008

Template:STRUCTURE 1js8

Structure of a Functional Unit from Octopus Hemocyanin


Overview

Hemocyanins are giant oxygen transport proteins found in many arthropods and molluscs. Freely dissolved in the hemolymph, they are multisubunit proteins that contain many copies of the active site, a copper atom pair that reversibly binds oxygen. Octopus hemocyanin is composed of ten subunits, each of which contain seven oxygen-binding "functional units". The carboxyl-terminal 47 kDa functional unit, Odg, is a proteolytic isolate that binds oxygen reversibly while exhibiting slight Bohr and magnesium ion effects. In this work we present the X-ray structure determination and analysis of Odg at 2.3 A resolution. Odg has two structural domains: a largely alpha-helical copper binding domain, and a five-stranded anti-parallel beta-sandwich with the jelly roll topology found in many viruses. Six histidine residues ligate the copper atoms, one of which is involved in a thioether bridge. The results show that the hemocyanin from the mollusc and that from the arthropod have distinct tertiary folds in addition to the long recognized differences in their quaternary structures. Nonetheless, a comparison of Octopus and horseshoe crab hemocyanin reveals a similar active site, in a striking example of perhaps both convergent and divergent evolution.

About this Structure

1JS8 is a Single protein structure of sequence from Octopus dofleini. Full crystallographic information is available from OCA.

Reference

Crystal structure of a functional unit from Octopus hemocyanin., Cuff ME, Miller KI, van Holde KE, Hendrickson WA, J Mol Biol. 1998 May 15;278(4):855-70. PMID:9614947 Page seeded by OCA on Fri May 2 21:49:39 2008

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