<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
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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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=1lnl ConSurf].
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Revision as of 14:31, 8 February 2016
Structure of deoxygenated hemocyanin from Rapana thomasiana
1lnl is a 3 chain structure with sequence from Rapana venosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
[HCY2E_RAPVE] Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.[UniProtKB:P12659]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Structure-function relationships in a molluscan hemocyanin have been investigated by determining the crystal structure of the Rapana thomasiana (gastropod) hemocyanin functional unit RtH2e in deoxygenated form at 3.38 A resolution. This is the first X-ray structure of an unit from the wall of the molluscan hemocyanin cylinder. The crystal structure of RtH2e demonstrates molecular self-assembly of six identical molecules forming a regular hexameric cylinder. This suggests how the functional units are ordered in the wall of the native molluscan hemocyanins. The molecular arrangement is stabilized by specific protomer-to-protomer interactions, which are probably typical for the functional units building the wall of the cylinders. A molecular mechanism for cooperative dioxygen binding in molluscan hemocyanins is proposed on the basis of the molecular interactions between the protomers. In particular, the deoxygenated RtH2e structure reveals a tunnel leading from two opposite sides of the molecule to the active site. The tunnel represents a possible entrance pathway for dioxygen molecules. No such tunnels have been observed in the crystal structure of the oxy-Odg, a functional unit from the Octopus dofleini (cephalopod) hemocyanin in oxygenated form.
The structure of a functional unit from the wall of a gastropod hemocyanin offers a possible mechanism for cooperativity.,Perbandt M, Guthohrlein EW, Rypniewski W, Idakieva K, Stoeva S, Voelter W, Genov N, Betzel C Biochemistry. 2003 Jun 3;42(21):6341-6. PMID:12767214[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑Perbandt M, Guthohrlein EW, Rypniewski W, Idakieva K, Stoeva S, Voelter W, Genov N, Betzel C. The structure of a functional unit from the wall of a gastropod hemocyanin offers a possible mechanism for cooperativity. Biochemistry. 2003 Jun 3;42(21):6341-6. PMID:12767214 doi:10.1021/bi020672x