1lnl
From Proteopedia
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|PDB= 1lnl |SIZE=350|CAPTION= <scene name='initialview01'>1lnl</scene>, resolution 3.30Å | |PDB= 1lnl |SIZE=350|CAPTION= <scene name='initialview01'>1lnl</scene>, resolution 3.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lnl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lnl OCA], [http://www.ebi.ac.uk/pdbsum/1lnl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lnl RCSB]</span> | ||
}} | }} | ||
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[[Category: Stoeva, S.]] | [[Category: Stoeva, S.]] | ||
[[Category: Voelter, W.]] | [[Category: Voelter, W.]] | ||
| - | [[Category: CU]] | ||
| - | [[Category: NAG]] | ||
[[Category: cooperativity]] | [[Category: cooperativity]] | ||
[[Category: copper]] | [[Category: copper]] | ||
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[[Category: oxygen]] | [[Category: oxygen]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:04:59 2008'' |
Revision as of 19:04, 30 March 2008
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| , resolution 3.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
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