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1w4u
From Proteopedia
| 1w4u, 10 NMR models () | |||||||||
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| Activity: | Ubiquitin--protein ligase, with EC number 6.3.2.19 | ||||||||
| Domains: | UBCc | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
NMR SOLUTION STRUCTURE OF THE UBIQUITIN CONJUGATING ENZYME UBCH5B
The ubiquitination pathway is the main pathway for protein degradation in eukaryotic cells. The attachment of ubiquitin to a substrate protein is catalyzed by three types of enzymes, namely a ubiquitin activating enzyme (E1), a ubiquitin-conjugating enzyme (E2), and a ubiquitin ligase (E3). Here, the structure of the human ubiquitin-conjugating enzyme (E2) UbcH5B has been solved by a combination of homology modeling, NMR relaxation data and automated NOE assignments. Comparison to E2 structures solved previously by X-ray crystallography or NMR shows in all cases the same compact fold, but differences are observed in the orientation of both N and C-terminal alpha-helices. The N-terminal helix that is involved in binding to ubiquitin ligases (E3) displays a different position, which could have consequences for precise E2-E3 recognition. In addition, multiple conformations of the side-chain of Asn77 are found in solution, which contrasts the single hydrogen-bonded conformation in the crystal structures of E2 enzymes. The possible implication of this conformational freedom of Asn77 for its catalytic function is discussed.
Solution structure of the ubiquitin-conjugating enzyme UbcH5B., Houben K, Dominguez C, van Schaik FM, Timmers HT, Bonvin AM, Boelens R, J Mol Biol. 2004 Nov 19;344(2):513-26. PMID:15522302
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1W4U is a 1 chain structure of sequence from Homo sapiens. Full experimental information is available from OCA.
Reference
- Houben K, Dominguez C, van Schaik FM, Timmers HT, Bonvin AM, Boelens R. Solution structure of the ubiquitin-conjugating enzyme UbcH5B. J Mol Biol. 2004 Nov 19;344(2):513-26. PMID:15522302 doi:10.1016/j.jmb.2004.09.054
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