2fuh

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[[Image:2fuh.gif|left|200px]]
[[Image:2fuh.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2fuh |SIZE=350|CAPTION= <scene name='initialview01'>2fuh</scene>
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The line below this paragraph, containing "STRUCTURE_2fuh", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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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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or leave the SCENE parameter empty for the default display.
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|GENE= UBE2D3, UBCH5C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), Rps27a, Uba80, Ubcep1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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-->
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|DOMAIN=
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{{STRUCTURE_2fuh| PDB=2fuh | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fuh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fuh OCA], [http://www.ebi.ac.uk/pdbsum/2fuh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fuh RCSB]</span>
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}}
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'''Solution Structure of the UbcH5c/Ub Non-covalent Complex'''
'''Solution Structure of the UbcH5c/Ub Non-covalent Complex'''
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[[Category: Klevit, R E.]]
[[Category: Klevit, R E.]]
[[Category: Lissounov, A.]]
[[Category: Lissounov, A.]]
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[[Category: protein-protein complex ubiquitin ubiquitin-conjugating enzyme]]
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[[Category: Protein-protein complex ubiquitin ubiquitin-conjugating enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:19:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:07:50 2008''
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Revision as of 01:19, 4 May 2008

Template:STRUCTURE 2fuh

Solution Structure of the UbcH5c/Ub Non-covalent Complex


Overview

Protein ubiquitination is a powerful regulatory modification that influences nearly every aspect of eukaryotic cell biology. The general pathway for ubiquitin (Ub) modification requires the sequential activities of a Ub-activating enzyme (E1), a Ub transfer enzyme (E2), and a Ub ligase (E3). The E2 must recognize both the E1 and a cognate E3 in addition to carrying activated Ub. These central functions are performed by a topologically conserved alpha/beta-fold core domain of approximately 150 residues shared by all E2s. However, as presented herein, the UbcH5 family of E2s can also bind Ub noncovalently on a surface well removed from the E2 active site. We present the solution structure of the UbcH5c/Ub noncovalent complex and demonstrate that this noncovalent interaction permits self-assembly of activated UbcH5c approximately Ub molecules. Self-assembly has profound consequences for the processive formation of polyubiquitin (poly-Ub) chains in ubiquitination reactions directed by the breast and ovarian cancer tumor susceptibility protein BRCA1.

About this Structure

2FUH is a Protein complex structure of sequences from Homo sapiens and Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

A UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination., Brzovic PS, Lissounov A, Christensen DE, Hoyt DW, Klevit RE, Mol Cell. 2006 Mar 17;21(6):873-80. PMID:16543155 Page seeded by OCA on Sun May 4 04:19:26 2008

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