1hwm
From Proteopedia
(New page: 200px<br /><applet load="1hwm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hwm, resolution 2.8Å" /> '''EBULIN,ORTHORHOMBIC C...) |
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| - | [[Image:1hwm.gif|left|200px]]<br /><applet load="1hwm" size=" | + | [[Image:1hwm.gif|left|200px]]<br /><applet load="1hwm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hwm, resolution 2.8Å" /> | caption="1hwm, resolution 2.8Å" /> | ||
'''EBULIN,ORTHORHOMBIC CRYSTAL FORM MODEL'''<br /> | '''EBULIN,ORTHORHOMBIC CRYSTAL FORM MODEL'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Ebulin l is a type-II ribosome-inactivating protein (RIP) isolated from | + | Ebulin l is a type-II ribosome-inactivating protein (RIP) isolated from the leaves of Sambucus ebulus L. As with other type-II RIP, ebulin is a disulfide-linked heterodimer composed of a toxic A chain and a galactoside-specific lectin B chain. A normal level of ribosome-inactivating N-glycosidase activity, characteristic of the A chain of type-II RIP, has been demonstrated for ebulin l. However, ebulin is considered a nontoxic type-II RIP due to a reduced cytotoxicity on whole cells and animals as compared with other toxic type-II RIP like ricin. The molecular cloning, amino acid sequence, and the crystal structure of ebulin l are presented and compared with ricin. Ebulin l is shown to bind an A-chain substrate analogue, pteroic acid, in the same manner as ricin. The galactoside-binding ability of ebulin l is demonstrated crystallographically with a complex of the B chain with galactose and with lactose. The negligible cytotoxicity of ebulin l is apparently due to a reduced affinity for galactosides. An altered mode of galactoside binding in the 2gamma subdomain of the lectin B chain primarily causes the reduced affinity. |
==About this Structure== | ==About this Structure== | ||
| - | 1HWM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sambucus_ebulus Sambucus ebulus] with GAL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1HWM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sambucus_ebulus Sambucus ebulus] with <scene name='pdbligand=GAL:'>GAL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HWM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Sambucus ebulus]] | [[Category: Sambucus ebulus]] | ||
[[Category: rRNA N-glycosylase]] | [[Category: rRNA N-glycosylase]] | ||
| - | [[Category: Day, P | + | [[Category: Day, P J.]] |
| - | [[Category: Ernst, S | + | [[Category: Ernst, S R.]] |
| - | [[Category: Monzingo, A | + | [[Category: Monzingo, A F.]] |
| - | [[Category: Pascal, J | + | [[Category: Pascal, J M.]] |
| - | [[Category: Robertus, J | + | [[Category: Robertus, J D.]] |
[[Category: GAL]] | [[Category: GAL]] | ||
[[Category: ribosome-inactivating protein]] | [[Category: ribosome-inactivating protein]] | ||
[[Category: ricin-like]] | [[Category: ricin-like]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:05:32 2008'' |
Revision as of 11:05, 21 February 2008
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EBULIN,ORTHORHOMBIC CRYSTAL FORM MODEL
Overview
Ebulin l is a type-II ribosome-inactivating protein (RIP) isolated from the leaves of Sambucus ebulus L. As with other type-II RIP, ebulin is a disulfide-linked heterodimer composed of a toxic A chain and a galactoside-specific lectin B chain. A normal level of ribosome-inactivating N-glycosidase activity, characteristic of the A chain of type-II RIP, has been demonstrated for ebulin l. However, ebulin is considered a nontoxic type-II RIP due to a reduced cytotoxicity on whole cells and animals as compared with other toxic type-II RIP like ricin. The molecular cloning, amino acid sequence, and the crystal structure of ebulin l are presented and compared with ricin. Ebulin l is shown to bind an A-chain substrate analogue, pteroic acid, in the same manner as ricin. The galactoside-binding ability of ebulin l is demonstrated crystallographically with a complex of the B chain with galactose and with lactose. The negligible cytotoxicity of ebulin l is apparently due to a reduced affinity for galactosides. An altered mode of galactoside binding in the 2gamma subdomain of the lectin B chain primarily causes the reduced affinity.
About this Structure
1HWM is a Protein complex structure of sequences from Sambucus ebulus with as ligand. Active as rRNA N-glycosylase, with EC number 3.2.2.22 Full crystallographic information is available from OCA.
Reference
2.8-A crystal structure of a nontoxic type-II ribosome-inactivating protein, ebulin l., Pascal JM, Day PJ, Monzingo AF, Ernst SR, Robertus JD, Iglesias R, Perez Y, Ferreras JM, Citores L, Girbes T, Proteins. 2001 May 15;43(3):319-26. PMID:11288182
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