1tbe
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tbe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tbe OCA], [http://www.ebi.ac.uk/pdbsum/1tbe PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tbe RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
Eukaryotic proteins are targeted for degradation by covalent ligation of multiubiquitin chains. In these multiubiquitin chains, successive ubiquitins are linked by an isopeptide bond involving the side chain of Lys48 and the carboxyl group of the C-terminus (Gly76). The crystal structure of a tetraubiquitin chain (Ub4) has been determined and refined at 2.4 A resolution. The molecule exhibits both translational and 2-fold rotational symmetry; each pair of (rotationally symmetric) ubiquitin molecules in Ub4 is related to the next pair by a simple translation. The 2-fold symmetry in each pair of ubiquitin molecules is quite different from the 2-fold symmetry observed in the previously determined structure of isolated diubiquitin. There are multiple hydrophilic contacts among the four ubiquitin molecules, but the hydrophobic surface formed in the middle of diubiquitin is not seen. The structure of the tetraubiquitin chain demonstrates how a multiubiquitin chain of any length can be formed. | Eukaryotic proteins are targeted for degradation by covalent ligation of multiubiquitin chains. In these multiubiquitin chains, successive ubiquitins are linked by an isopeptide bond involving the side chain of Lys48 and the carboxyl group of the C-terminus (Gly76). The crystal structure of a tetraubiquitin chain (Ub4) has been determined and refined at 2.4 A resolution. The molecule exhibits both translational and 2-fold rotational symmetry; each pair of (rotationally symmetric) ubiquitin molecules in Ub4 is related to the next pair by a simple translation. The 2-fold symmetry in each pair of ubiquitin molecules is quite different from the 2-fold symmetry observed in the previously determined structure of isolated diubiquitin. There are multiple hydrophilic contacts among the four ubiquitin molecules, but the hydrophobic surface formed in the middle of diubiquitin is not seen. The structure of the tetraubiquitin chain demonstrates how a multiubiquitin chain of any length can be formed. | ||
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| - | ==Disease== | ||
| - | Known disease associated with this structure: Cleft palate, isolated OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191339 191339]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: ubiquitin]] | [[Category: ubiquitin]] | ||
| - | ''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 23:53:49 2008'' |
Revision as of 20:53, 30 March 2008
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| , resolution 2.4Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF TETRAUBIQUITIN SHOWS HOW MULTIUBIQUITIN CHAINS CAN BE FORMED
Overview
Eukaryotic proteins are targeted for degradation by covalent ligation of multiubiquitin chains. In these multiubiquitin chains, successive ubiquitins are linked by an isopeptide bond involving the side chain of Lys48 and the carboxyl group of the C-terminus (Gly76). The crystal structure of a tetraubiquitin chain (Ub4) has been determined and refined at 2.4 A resolution. The molecule exhibits both translational and 2-fold rotational symmetry; each pair of (rotationally symmetric) ubiquitin molecules in Ub4 is related to the next pair by a simple translation. The 2-fold symmetry in each pair of ubiquitin molecules is quite different from the 2-fold symmetry observed in the previously determined structure of isolated diubiquitin. There are multiple hydrophilic contacts among the four ubiquitin molecules, but the hydrophobic surface formed in the middle of diubiquitin is not seen. The structure of the tetraubiquitin chain demonstrates how a multiubiquitin chain of any length can be formed.
About this Structure
1TBE is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of tetraubiquitin shows how multiubiquitin chains can be formed., Cook WJ, Jeffrey LC, Kasperek E, Pickart CM, J Mol Biol. 1994 Feb 18;236(2):601-9. PMID:8107144
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