1ulm: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /><applet load="1ulm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ulm, resolution 1.80Å" /> '''Crystal Structure of...
 
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:1ulm.jpg|left|200px]]<br /><applet load="1ulm" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1ulm.jpg|left|200px]]<br /><applet load="1ulm" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1ulm, resolution 1.80&Aring;" />
caption="1ulm, resolution 1.80&Aring;" />
'''Crystal Structure of Pokeweed Lectin-D2 complexed with tri-N-acetylchitotriose'''<br />
'''Crystal Structure of Pokeweed Lectin-D2 complexed with tri-N-acetylchitotriose'''<br />


==Overview==
==Overview==
The roots of pokeweed (Phytolacca americana) are known to contain the, lectins designated PL-A, PL-B, PL-C, PL-D1, and PL-D2. Of these lectins, the crystal structures of two PLs, the ligand-free PL-C and the complex of, PL-D2 with tri-N-acetylchitotriose, have been determined at 1.8A, resolution. The polypeptide chains of PL-C and PL-D2 form three and two, repetitive chitin-binding domains, respectively. In the crystal structure, of the PL-D2 complex, one trisaccharide molecule is shared mainly between, two neighboring molecules related to each other by a crystallographic, 2(1)-screw axis, and infinite helical chains of complexed molecules are, generated by the sharing of ligand molecules. The crystal structure of, PL-C reveals that the molecule is a dimer of two identical subunits, whose, polypeptide chains are located in a head-to-tail fashion by a molecular, 2-fold axis. Three putative carbohydrate-binding sites in each subunit are, located in the dimer interface. The dimerization of PL-C is performed, through the hydrophobic interactions between the carbohydrate-binding, sites of the opposite domains in the dimer, leading to a distinct, dimerization mode from that of wheat-germ agglutinin. Three aromatic, residues in each carbohydrate-binding site of PL-C are involved in the, dimerization. These residues correspond to the residues that interact, mainly with the trisaccharide in the PL-D2 complex and appear to mimic the, saccharide residues in the complex. Consequently, the present structure of, the PL-C dimer has no room for accommodating carbohydrate. The quaternary, structure of PL-C formed through these putative carbohydrate-binding, residues may lead to the lack of hemagglutinating activity.
The roots of pokeweed (Phytolacca americana) are known to contain the lectins designated PL-A, PL-B, PL-C, PL-D1, and PL-D2. Of these lectins, the crystal structures of two PLs, the ligand-free PL-C and the complex of PL-D2 with tri-N-acetylchitotriose, have been determined at 1.8A resolution. The polypeptide chains of PL-C and PL-D2 form three and two repetitive chitin-binding domains, respectively. In the crystal structure of the PL-D2 complex, one trisaccharide molecule is shared mainly between two neighboring molecules related to each other by a crystallographic 2(1)-screw axis, and infinite helical chains of complexed molecules are generated by the sharing of ligand molecules. The crystal structure of PL-C reveals that the molecule is a dimer of two identical subunits, whose polypeptide chains are located in a head-to-tail fashion by a molecular 2-fold axis. Three putative carbohydrate-binding sites in each subunit are located in the dimer interface. The dimerization of PL-C is performed through the hydrophobic interactions between the carbohydrate-binding sites of the opposite domains in the dimer, leading to a distinct dimerization mode from that of wheat-germ agglutinin. Three aromatic residues in each carbohydrate-binding site of PL-C are involved in the dimerization. These residues correspond to the residues that interact mainly with the trisaccharide in the PL-D2 complex and appear to mimic the saccharide residues in the complex. Consequently, the present structure of the PL-C dimer has no room for accommodating carbohydrate. The quaternary structure of PL-C formed through these putative carbohydrate-binding residues may lead to the lack of hemagglutinating activity.


==About this Structure==
==About this Structure==
1ULM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Phytolacca_americana Phytolacca americana]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ULM OCA].  
1ULM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Phytolacca_americana Phytolacca americana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ULM OCA].  


==Reference==
==Reference==
Line 21: Line 21:
[[Category: lectin]]
[[Category: lectin]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:13:41 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:25:50 2008''