This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1oql
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1oql.gif|left|200px]] | + | [[Image:1oql.gif|left|200px]] |
| - | + | ||
| - | '''Mistletoe Lectin I from Viscum album complexed with galactose''' | + | {{Structure |
| + | |PDB= 1oql |SIZE=350|CAPTION= <scene name='initialview01'>1oql</scene>, resolution 3.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene> and <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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Mistletoe Lectin I from Viscum album complexed with galactose''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1OQL is a [ | + | 1OQL is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Viscum_album Viscum album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OQL OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12823544 12823544] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Viscum album]] | [[Category: Viscum album]] | ||
| Line 26: | Line 35: | ||
[[Category: type-ii ribosome-inactivating protein]] | [[Category: type-ii ribosome-inactivating protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:14:17 2008'' |
Revision as of 11:14, 20 March 2008
| |||||||
| , resolution 3.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | rRNA N-glycosylase, with EC number 3.2.2.22 | ||||||
| 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
Page seeded by OCA on Thu Mar 20 13:14:17 2008
