1oql
From Proteopedia
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|PDB= 1oql |SIZE=350|CAPTION= <scene name='initialview01'>1oql</scene>, resolution 3.0Å | |PDB= 1oql |SIZE=350|CAPTION= <scene name='initialview01'>1oql</scene>, resolution 3.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene> | + | |LIGAND= <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/rRNA_N-glycosylase rRNA N-glycosylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.22 3.2.2.22] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/rRNA_N-glycosylase rRNA N-glycosylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.22 3.2.2.22] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oql OCA], [http://www.ebi.ac.uk/pdbsum/1oql PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oql RCSB]</span> | ||
}} | }} | ||
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[[Category: Saward, S.]] | [[Category: Saward, S.]] | ||
[[Category: Tonevitsky, A G.]] | [[Category: Tonevitsky, A G.]] | ||
| - | [[Category: GAL]] | ||
| - | [[Category: NAG]] | ||
[[Category: beta-trefoil]] | [[Category: beta-trefoil]] | ||
[[Category: ricin-like]] | [[Category: ricin-like]] | ||
[[Category: type-ii ribosome-inactivating protein]] | [[Category: type-ii ribosome-inactivating protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:48:54 2008'' |
Revision as of 19:48, 30 March 2008
| |||||||
| , resolution 3.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | rRNA N-glycosylase, with EC number 3.2.2.22 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Mistletoe Lectin I from Viscum album complexed with galactose
Overview
The X-ray structure of mistletoe lectin I (MLI), a type-II ribosome-inactivating protein (RIP), cocrystallized with galactose is described. The model was refined at 3.0 A resolution to an R-factor of 19.9% using 21 899 reflections, with Rfree 24.0%. MLI forms a homodimer (A-B)2 in the crystal, as it does in solution at high concentration. The dimer is formed through contacts between the N-terminal domains of two B-chains involving weak polar and non-polar interactions. Consequently, the overall arrangement of sugar-binding sites in MLI differs from those in monomeric type-II RIPs: two N-terminal sugar-binding sites are 15 A apart on one side of the dimer, and two C-terminal sugar-binding sites are 87 A apart on the other side. Galactose binding is achieved by common hydrogen bonds for the two binding sites via hydroxy groups 3-OH and 4-OH and hydrophobic contact by an aromatic ring. In addition, at the N-terminal site 2-OH forms hydrogen bonds with Asp27 and Lys41, and at the C-terminal site 3-OH and 6-OH undergo water-mediated interactions and C5 has a hydrophobic contact. MLI is a galactose-specific lectin and shows little affinity for N-acetylgalactosamine. The reason for this is discussed. Structural differences among the RIPs investigated in this study (their quaternary structures, location of sugar-binding sites, and fine sugar specificities of their B-chains, which could have diverged through evolution from a two-domain protein) may affect the binding sites, and consequently the cellular transport processes and biological responses of these toxins.
About this Structure
1OQL is a Protein complex structure of sequences from Viscum album. Full crystallographic information is available from OCA.
Reference
Crystal structure at 3 A of mistletoe lectin I, a dimeric type-II ribosome-inactivating protein, complexed with galactose., Niwa H, Tonevitsky AG, Agapov II, Saward S, Pfuller U, Palmer RA, Eur J Biochem. 2003 Jul;270(13):2739-49. PMID:12823544
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