From Proteopedia
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| - | [[Image:2z49.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2z49| PDB=2z49 | SCENE= }} | | {{STRUCTURE_2z49| PDB=2z49 | SCENE= }} |
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| - | '''Crystal Structure of Hemolytic Lectin CEL-III Complexed with methyl-alpha-D-galactopylanoside'''
| + | ===Crystal Structure of Hemolytic Lectin CEL-III Complexed with methyl-alpha-D-galactopylanoside=== |
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| - | ==Overview==
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| - | CEL-III is a Ca(2+)-dependent hemolytic lectin, isolated from the marine invertebrate Cucumaria echinata. The three-dimensional structure of CEL-III/GalNAc and CEL-III/methyl alpha-galactoside complexes was solved by x-ray crystallographic analysis. In these complexes, five carbohydrate molecules were found to be bound to two carbohydrate-binding domains (domains 1 and 2) located in the N-terminal 2/3 portion of the polypeptide and that contained beta-trefoil folds similar to ricin B-chain. The 3-OH and 4-OH of bound carbohydrate molecules were coordinated with Ca(2+) located at the subdomains 1alpha, 1gamma, 2alpha, 2beta, and 2gamma, simultaneously forming hydrogen bond networks with nearby amino acid side chains, which is similar to carbohydrate binding in C-type lectins. The binding of carbohydrates was further stabilized by aromatic amino acid residues, such as tyrosine and tryptophan, through a stacking interaction with the hydrophobic face of carbohydrates. The importance of amino acid residues in the carbohydrate-binding sites was confirmed by the mutational analyses. The orientation of bound GalNAc and methyl alpha-galactoside was similar to the galactose moiety of lactose bound to the carbohydrate-binding site of the ricin B-chain, although the ricin B-chain does not require Ca(2+) ions for carbohydrate binding. The binding of the carbohydrates induced local structural changes in carbohydrate-binding sites in subdomains 2alpha and 2beta. Binding of GalNAc also induced a slight change in the main chain structure of domain 3, which could be related to the conformational change upon binding of specific carbohydrates to induce oligomerization of the protein.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17977832}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17977832 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17977832}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Pore-forming]] | | [[Category: Pore-forming]] |
| | [[Category: Toxin]] | | [[Category: Toxin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 19:56:17 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:54:12 2008'' |
Revision as of 00:54, 28 July 2008
Template:STRUCTURE 2z49
Crystal Structure of Hemolytic Lectin CEL-III Complexed with methyl-alpha-D-galactopylanoside
Template:ABSTRACT PUBMED 17977832
About this Structure
2Z49 is a Single protein structure of sequence from Cucumaria echinata. Full crystallographic information is available from OCA.
Reference
C-type lectin-like carbohydrate recognition of the hemolytic lectin CEL-III containing ricin-type -trefoil folds., Hatakeyama T, Unno H, Kouzuma Y, Uchida T, Eto S, Hidemura H, Kato N, Yonekura M, Kusunoki M, J Biol Chem. 2007 Dec 28;282(52):37826-35. Epub 2007 Oct 31. PMID:17977832
Page seeded by OCA on Mon Jul 28 03:54:12 2008
