1w4u

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[[Image:1w4u.gif|left|200px]]
[[Image:1w4u.gif|left|200px]]
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{{Structure
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|PDB= 1w4u |SIZE=350|CAPTION= <scene name='initialview01'>1w4u</scene>
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The line below this paragraph, containing "STRUCTURE_1w4u", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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{{STRUCTURE_1w4u| PDB=1w4u | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w4u OCA], [http://www.ebi.ac.uk/pdbsum/1w4u PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w4u RCSB]</span>
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'''NMR SOLUTION STRUCTURE OF THE UBIQUITIN CONJUGATING ENZYME UBCH5B'''
'''NMR SOLUTION STRUCTURE OF THE UBIQUITIN CONJUGATING ENZYME UBCH5B'''
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[[Category: Schaik, F M.A Van.]]
[[Category: Schaik, F M.A Van.]]
[[Category: Timmers, H T.M.]]
[[Category: Timmers, H T.M.]]
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[[Category: bl conjugation pathway]]
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[[Category: Bl conjugation pathway]]
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[[Category: e2 enzyme]]
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[[Category: E2 enzyme]]
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[[Category: ligase]]
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[[Category: Ligase]]
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[[Category: ubiquitination]]
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[[Category: Ubiquitination]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:09:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:31:10 2008''
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Revision as of 10:09, 3 May 2008

Image:1w4u.gif

Template:STRUCTURE 1w4u

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 Page seeded by OCA on Sat May 3 13:09:36 2008

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