1tlg: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /><applet load="1tlg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tlg, resolution 2.2Å" /> '''STRUCTURE OF A TUNICA...
 
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:1tlg.jpg|left|200px]]<br /><applet load="1tlg" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1tlg.jpg|left|200px]]<br /><applet load="1tlg" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1tlg, resolution 2.2&Aring;" />
caption="1tlg, resolution 2.2&Aring;" />
'''STRUCTURE OF A TUNICATE C-TYPE LECTIN COMPLEXED WITH D-GALACTOSE'''<br />
'''STRUCTURE OF A TUNICATE C-TYPE LECTIN COMPLEXED WITH D-GALACTOSE'''<br />


==Overview==
==Overview==
C-type lectins are calcium-dependent carbohydrate-recognising proteins., Isothermal titration calorimetry of the C-type Polyandrocarpa lectin, (TC14) from the tunicate Polyandrocarpa misakiensis revealed the presence, of a single calcium atom per monomer with a dissociation constant of 2.6, microM, and confirmed the specificity of TC14 for D -galactose and related, monosaccharides. We have determined the 2.2 A X-ray crystal structure of, Polyandrocarpa lectin complexed with D -galactose. Analytical, ultracentrifugation revealed that TC14 behaves as a dimer in solution., This is reflected by the presence of two molecules in the asymmetric unit, with the dimeric interface formed by antiparallel pairing of the two, N-terminal beta-strands and hydrophobic interactions. TC14 adopts a, typical C-type lectin fold with differences in structure from other C-type, lectins mainly in the diverse loop regions and in the second alpha-helix, which is involved in the formation of the dimeric interface. The D, -galactose is bound through coordination of the 3 and 4-hydroxyl oxygen, atoms with a bound calcium atom. Additional hydrogen bonds are formed, directly between serine, aspartate and glutamate side-chains of the, protein and the sugar 3 and 4-hydroxyl groups. Comparison of the galactose, binding by TC14 with the mannose binding by rat mannose-binding protein, reveals how monosaccharide specificity is achieved in this lectin. A, tryptophan side-chain close to the binding site and the distribution of, hydrogen-bond acceptors and donors around the 3 and 4-hydroxyl groups of, the sugar are essential determinants of specificity. These elements are, however, arranged in a very different way than in an engineered, galactose-specific mutant of MBPA. Possible biological functions can more, easily be understood from the fact that TC14 is a dimer under, physiological conditions.
C-type lectins are calcium-dependent carbohydrate-recognising proteins. Isothermal titration calorimetry of the C-type Polyandrocarpa lectin (TC14) from the tunicate Polyandrocarpa misakiensis revealed the presence of a single calcium atom per monomer with a dissociation constant of 2.6 microM, and confirmed the specificity of TC14 for D -galactose and related monosaccharides. We have determined the 2.2 A X-ray crystal structure of Polyandrocarpa lectin complexed with D -galactose. Analytical ultracentrifugation revealed that TC14 behaves as a dimer in solution. This is reflected by the presence of two molecules in the asymmetric unit with the dimeric interface formed by antiparallel pairing of the two N-terminal beta-strands and hydrophobic interactions. TC14 adopts a typical C-type lectin fold with differences in structure from other C-type lectins mainly in the diverse loop regions and in the second alpha-helix, which is involved in the formation of the dimeric interface. The D -galactose is bound through coordination of the 3 and 4-hydroxyl oxygen atoms with a bound calcium atom. Additional hydrogen bonds are formed directly between serine, aspartate and glutamate side-chains of the protein and the sugar 3 and 4-hydroxyl groups. Comparison of the galactose binding by TC14 with the mannose binding by rat mannose-binding protein reveals how monosaccharide specificity is achieved in this lectin. A tryptophan side-chain close to the binding site and the distribution of hydrogen-bond acceptors and donors around the 3 and 4-hydroxyl groups of the sugar are essential determinants of specificity. These elements are, however, arranged in a very different way than in an engineered galactose-specific mutant of MBPA. Possible biological functions can more easily be understood from the fact that TC14 is a dimer under physiological conditions.


==About this Structure==
==About this Structure==
1TLG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Polyandrocarpa_misakiensis Polyandrocarpa misakiensis] with GAL, CA and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TLG OCA].  
1TLG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Polyandrocarpa_misakiensis Polyandrocarpa misakiensis] with <scene name='pdbligand=GAL:'>GAL</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TLG OCA].  


==Reference==
==Reference==
Line 14: Line 14:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bycroft, M.]]
[[Category: Bycroft, M.]]
[[Category: Legge, G.B.]]
[[Category: Legge, G B.]]
[[Category: Poget, S.F.]]
[[Category: Poget, S F.]]
[[Category: Williams, R.L.]]
[[Category: Williams, R L.]]
[[Category: CA]]
[[Category: CA]]
[[Category: GAL]]
[[Category: GAL]]
Line 24: Line 24:
[[Category: galactose-specific]]
[[Category: galactose-specific]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:22:42 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:14:46 2008''