2fuh
From Proteopedia
(New page: 200px<br /> <applet load="2fuh" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fuh" /> '''Solution Structure of the UbcH5c/Ub Non-cov...) |
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'''Solution Structure of the UbcH5c/Ub Non-covalent Complex'''<br /> | '''Solution Structure of the UbcH5c/Ub Non-covalent Complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Protein ubiquitination is a powerful regulatory modification that | + | 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. |
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| + | ==Disease== | ||
| + | Known disease associated with this structure: Cleft palate, isolated OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191339 191339]] | ||
==About this Structure== | ==About this Structure== | ||
| - | 2FUH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. 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:// | + | 2FUH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. 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=2FUH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Ubiquitin--protein ligase]] | [[Category: Ubiquitin--protein ligase]] | ||
| - | [[Category: Brzovic, P | + | [[Category: Brzovic, P S.]] |
| - | [[Category: Hoyt, D | + | [[Category: Hoyt, D W.]] |
| - | [[Category: Klevit, R | + | [[Category: Klevit, R E.]] |
[[Category: Lissounov, A.]] | [[Category: Lissounov, A.]] | ||
[[Category: protein-protein complex ubiquitin ubiquitin-conjugating enzyme]] | [[Category: protein-protein complex ubiquitin ubiquitin-conjugating enzyme]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:25:12 2008'' |
Revision as of 15:25, 21 February 2008
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Solution Structure of the UbcH5c/Ub Non-covalent Complex
Contents |
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.
Disease
Known disease associated with this structure: Cleft palate, isolated OMIM:[191339]
About this Structure
2FUH is a Protein complex structure of sequences from Homo sapiens and Rattus norvegicus. Active as Ubiquitin--protein ligase, with EC number 6.3.2.19 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
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