1w4u
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(New page: 200px<br /> <applet load="1w4u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w4u" /> '''NMR SOLUTION STRUCTURE OF THE UBIQUITIN CON...)
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Revision as of 17:40, 12 November 2007
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NMR SOLUTION STRUCTURE OF THE UBIQUITIN CONJUGATING ENZYME UBCH5B
Overview
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.
About this Structure
1W4U is a Single protein structure of sequence from Homo sapiens. Active as Ubiquitin--protein ligase, with EC number 6.3.2.19 Full crystallographic information is available from OCA.
Reference
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
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