1w4u
From Proteopedia
(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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'''NMR SOLUTION STRUCTURE OF THE UBIQUITIN CONJUGATING ENZYME UBCH5B'''<br /> | '''NMR SOLUTION STRUCTURE OF THE UBIQUITIN CONJUGATING ENZYME UBCH5B'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The ubiquitination pathway is the main pathway for protein degradation in | + | 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== | ==About this Structure== | ||
| - | 1W4U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [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] Full crystallographic information is available from [http:// | + | 1W4U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W4U OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ubiquitin--protein ligase]] | [[Category: Ubiquitin--protein ligase]] | ||
[[Category: Boelens, R.]] | [[Category: Boelens, R.]] | ||
| - | [[Category: Bonvin, A | + | [[Category: Bonvin, A M.J J.]] |
[[Category: Dominguez, C.]] | [[Category: Dominguez, C.]] | ||
[[Category: Houben, K.]] | [[Category: Houben, K.]] | ||
| - | [[Category: Schaik, F | + | [[Category: Schaik, F M.A Van.]] |
| - | [[Category: Timmers, H | + | [[Category: Timmers, H T.M.]] |
[[Category: bl conjugation pathway]] | [[Category: bl conjugation pathway]] | ||
[[Category: e2 enzyme]] | [[Category: e2 enzyme]] | ||
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[[Category: ubiquitination]] | [[Category: ubiquitination]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:40:29 2008'' |
Revision as of 13:40, 21 February 2008
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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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