1w4u: Difference between revisions
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[[Image:1w4u.gif|left|200px]] | [[Image:1w4u.gif|left|200px]] | ||
'''NMR SOLUTION STRUCTURE OF THE UBIQUITIN CONJUGATING ENZYME UBCH5B''' | {{Structure | ||
|PDB= 1w4u |SIZE=350|CAPTION= <scene name='initialview01'>1w4u</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] | |||
|GENE= | |||
}} | |||
'''NMR SOLUTION STRUCTURE OF THE UBIQUITIN CONJUGATING ENZYME UBCH5B''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1W4U is a [ | 1W4U is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W4U OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15522302 15522302] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ubiquitination]] | [[Category: ubiquitination]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:52:14 2008'' | ||
Revision as of 12:52, 20 March 2008
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| Activity: | Ubiquitin--protein ligase, with EC number 6.3.2.19 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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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