1vcl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1vcl.gif|left|200px]]<br /><applet load="1vcl" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1vcl.gif|left|200px]]
-
caption="1vcl, resolution 1.70&Aring;" />
+
 
-
'''Crystal Structure of Hemolytic Lectin CEL-III'''<br />
+
{{Structure
 +
|PDB= 1vcl |SIZE=350|CAPTION= <scene name='initialview01'>1vcl</scene>, resolution 1.70&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>
 +
|ACTIVITY=
 +
|GENE=
 +
}}
 +
 
 +
'''Crystal Structure of Hemolytic Lectin CEL-III'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1VCL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cucumaria_echinata Cucumaria echinata] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=BTB:'>BTB</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VCL OCA].
+
1VCL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cucumaria_echinata Cucumaria echinata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VCL OCA].
==Reference==
==Reference==
-
Crystal structure of the hemolytic lectin CEL-III isolated from the marine invertebrate Cucumaria echinata: implications of domain structure for its membrane pore-formation mechanism., Uchida T, Yamasaki T, Eto S, Sugawara H, Kurisu G, Nakagawa A, Kusunoki M, Hatakeyama T, J Biol Chem. 2004 Aug 27;279(35):37133-41. Epub 2004 Jun 11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15194688 15194688]
+
Crystal structure of the hemolytic lectin CEL-III isolated from the marine invertebrate Cucumaria echinata: implications of domain structure for its membrane pore-formation mechanism., Uchida T, Yamasaki T, Eto S, Sugawara H, Kurisu G, Nakagawa A, Kusunoki M, Hatakeyama T, J Biol Chem. 2004 Aug 27;279(35):37133-41. Epub 2004 Jun 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15194688 15194688]
[[Category: Cucumaria echinata]]
[[Category: Cucumaria echinata]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 32: Line 41:
[[Category: pore-forming]]
[[Category: pore-forming]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:33:52 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:43:48 2008''

Revision as of 12:43, 20 March 2008

Image:1vcl.gif


PDB ID 1vcl

Drag the structure with the mouse to rotate
, resolution 1.70Å
Ligands: , , and
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of Hemolytic Lectin CEL-III


Overview

CEL-III is a Ca(2+)-dependent and galactose-specific lectin purified from the sea cucumber, Cucumaria echinata, which exhibits hemolytic and hemagglutinating activities. Six molecules of CEL-III are assumed to oligomerize to form an ion-permeable pore in the cell membrane. We have determined the crystal structure of CELIII by using single isomorphous replacement aided by anomalous scattering in lead at 1.7 A resolution. CEL-III consists of three distinct domains as follows: the N-terminal two carbohydrate-binding domains (1 and 2), which adopt beta-trefoil folds such as the B-chain of ricin and are members of the (QXW)(3) motif family; and domain 3, which is a novel fold composed of two alpha-helices and one beta-sandwich. CEL-III is the first Ca(2+)-dependent lectin structure with two beta-trefoil folds. Despite sharing the structure of the B-chain of ricin, CEL-III binds five Ca(2+) ions at five of the six subdomains in both domains 1 and 2. Considering the relatively high similarity among the five subdomains, they are putative binding sites for galactose-related carbohydrates, although it remains to be elucidated whether bound Ca(2+) is directly involved in interaction with carbohydrates. The paucity of hydrophobic interactions in the interfaces between the domains and biochemical data suggest that these domains rearrange upon carbohydrate binding in the erythrocyte membrane. This conformational change may be responsible for oligomerization of CEL-III molecules and hemolysis in the erythrocyte membranes.

About this Structure

1VCL is a Single protein structure of sequence from Cucumaria echinata. Full crystallographic information is available from OCA.

Reference

Crystal structure of the hemolytic lectin CEL-III isolated from the marine invertebrate Cucumaria echinata: implications of domain structure for its membrane pore-formation mechanism., Uchida T, Yamasaki T, Eto S, Sugawara H, Kurisu G, Nakagawa A, Kusunoki M, Hatakeyama T, J Biol Chem. 2004 Aug 27;279(35):37133-41. Epub 2004 Jun 11. PMID:15194688

Page seeded by OCA on Thu Mar 20 14:43:48 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1vcl"
Personal tools