4e0q
From Proteopedia
Crystal structure of MPN domain from COP9 signalosome
Structural highlights
Function[CSN6_DROME] Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF. The CSN complex plays an essential role in oogenesis and embryogenesis and is required for proper photoreceptor R cell differentiation and promote lamina glial cell migration or axon targeting. It also promotes Ubl-dependent degradation of cyclin E (CycE) during early oogenesis.[1] Publication Abstract from PubMedThe COP9 signalosome (CSN) is a multiprotein complex containing eight subunits and is highly conserved from fungi to human. CSN is proposed to widely participate in many physiological processes, including protein degradation, DNA damage response and signal transduction. Among those subunits, only CSN5 and CSN6 belong to JAMM family. CSN5 possesses isopeptidase activity, but CSN6 lacks this ability. Here we report the 2.5A crystal structure of MPN domain from Drosophila melanogaster CSN6. Structural comparison with other MPN domains, along with bioinformation analysis, suggests that MPN domain from CSN6 may serve as a scaffold instead of a metalloprotease. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: CSN6 and CSN6bind by x-ray crystallography (View interaction) CSN6 and CSN6bind by x ray scattering (View interaction). The crystal structure of the MPN domain from the COP9 signalosome subunit CSN6.,Zhang H, Gao ZQ, Wang WJ, Liu GF, Shtykova EV, Xu JH, Li LF, Su XD, Dong YH FEBS Lett. 2012 Apr 24;586(8):1147-53. Epub 2012 Mar 23. PMID:22575649[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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