1W4U

NMR solution structure of the ubiquitin conjugating enzyme UbcH5B

Summary for 1W4U

• Entry DOI: 10.2210/pdb1w4u/pdb
• Related: 1UR6
• Descriptor: UBIQUITIN-CONJUGATING ENZYME E2-17 KDA 2 (1 entity in total)
• Functional Keywords: ubiquitination, e2 enzyme, ligase, bl conjugation pathway
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 1
• Total formula weight: 16755.23

Authors

Houben, K.,Dominguez, C.,Van Schaik, F.M.A.,Timmers, H.T.M.,Bonvin, A.M.J.J.,Boelens, R. (deposition date: 2004-07-29, release date: 2004-11-10, Last modification date: 2024-05-15)

Primary citation

Houben, K.,Dominguez, C.,Van Schaik, F.M.A.,Timmers, H.T.M.,Bonvin, A.M.J.J.,Boelens, R.
Solution Structure of the Ubiquitin-Conjugating Enzyme Ubch5B
J.Mol.Biol., 344:513-, 2004

PubMed Abstract: 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.

PubMed: 15522302
DOI: 10.1016/J.JMB.2004.09.054

Experimental method

SOLUTION NMR