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New page: left|200px<br /><applet load="1lnl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lnl, resolution 3.30Å" /> '''Structure of deoxyge...
 
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[[Image:1lnl.gif|left|200px]]<br /><applet load="1lnl" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1lnl, resolution 3.30&Aring;" />
'''Structure of deoxygenated hemocyanin from Rapana thomasiana'''<br />


==Overview==
==Structure of deoxygenated hemocyanin from Rapana thomasiana==
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.
<StructureSection load='1lnl' size='340' side='right'caption='[[1lnl]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1lnl]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Rapana_venosa Rapana venosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LNL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LNL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lnl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lnl OCA], [https://pdbe.org/1lnl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lnl RCSB], [https://www.ebi.ac.uk/pdbsum/1lnl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lnl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HCY2E_RAPVE HCY2E_RAPVE] Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.[UniProtKB:P12659]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ln/1lnl_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==About this Structure==
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<ref>PMID:12767214</ref>
1LNL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rapana_thomasiana Rapana thomasiana] with NAG and CU as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LNL OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12767214 12767214]
</div>
[[Category: Rapana thomasiana]]
<div class="pdbe-citations 1lnl" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
== References ==
[[Category: Betzel, C.]]
<references/>
[[Category: Genov, N.]]
__TOC__
[[Category: Guthoehrlein, E.W.]]
</StructureSection>
[[Category: Idakieva, K.]]
[[Category: Large Structures]]
[[Category: Perbandt, M.]]
[[Category: Rapana venosa]]
[[Category: Rypniewski, W.]]
[[Category: Betzel C]]
[[Category: Stoeva, S.]]
[[Category: Genov N]]
[[Category: Voelter, W.]]
[[Category: Guthoehrlein EW]]
[[Category: CU]]
[[Category: Idakieva K]]
[[Category: NAG]]
[[Category: Perbandt M]]
[[Category: cooperativity]]
[[Category: Rypniewski W]]
[[Category: copper]]
[[Category: Stoeva S]]
[[Category: deoxygenated form]]
[[Category: Voelter W]]
[[Category: hemocyanin]]
[[Category: metal binding site]]
[[Category: oxygen]]
 
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