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1lnl
From Proteopedia
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| - | [[Image:1lnl.gif|left|200px]] | + | [[Image:1lnl.gif|left|200px]] |
| - | + | ||
| - | '''Structure of deoxygenated hemocyanin from Rapana thomasiana''' | + | {{Structure |
| + | |PDB= 1lnl |SIZE=350|CAPTION= <scene name='initialview01'>1lnl</scene>, resolution 3.30Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=CU:COPPER (II) ION'>CU</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structure of deoxygenated hemocyanin from Rapana thomasiana''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1LNL is a [ | + | 1LNL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rapana_thomasiana Rapana thomasiana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LNL OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12767214 12767214] |
[[Category: Rapana thomasiana]] | [[Category: Rapana thomasiana]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: oxygen]] | [[Category: oxygen]] | ||
| - | ''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 12:32:58 2008'' |
Revision as of 10:32, 20 March 2008
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| , resolution 3.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of deoxygenated hemocyanin from Rapana thomasiana
Overview
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.
About this Structure
1LNL is a Single protein structure of sequence from Rapana thomasiana. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 12:32:58 2008
Categories: Rapana thomasiana | Single protein | Betzel, C. | Genov, N. | Guthoehrlein, E W. | Idakieva, K. | Perbandt, M. | Rypniewski, W. | Stoeva, S. | Voelter, W. | CU | NAG | Cooperativity | Copper | Deoxygenated form | Hemocyanin | Metal binding site | Oxygen
