1js8
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1js8.gif|left|200px]] | + | [[Image:1js8.gif|left|200px]] |
| - | + | ||
| - | '''Structure of a Functional Unit from Octopus Hemocyanin''' | + | {{Structure |
| + | |PDB= 1js8 |SIZE=350|CAPTION= <scene name='initialview01'>1js8</scene>, resolution 2.3Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene> and <scene name='pdbligand=CUO:CU2-O2 CLUSTER'>CUO</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structure of a Functional Unit from Octopus Hemocyanin''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1JS8 is a [ | + | 1JS8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Octopus_dofleini Octopus dofleini]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JS8 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9614947 9614947] |
[[Category: Octopus dofleini]] | [[Category: Octopus dofleini]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 25: | Line 34: | ||
[[Category: thioether bond]] | [[Category: thioether bond]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:07:44 2008'' |
Revision as of 10:07, 20 March 2008
| |||||||
| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 12:07:44 2008
