4E0Q

Crystal structure of MPN domain from COP9 signalosome

Summary for 4E0Q

• Entry DOI: 10.2210/pdb4e0q/pdb
• Descriptor: COP9 signalosome complex subunit 6 (2 entities in total)
• Functional Keywords: mpn (mpr1p and pad1p n-terminal) domain, unknown function
• Biological source: Drosophila melanogaster (Fruit fly)
• Cellular location: Cytoplasm (Probable): Q9VCY3
• Total number of polymer chains: 2
• Total formula weight: 32878.13

Authors

Zhang, H.,Gao, Z.Q.,Dong, Y.H. (deposition date: 2012-03-05, release date: 2012-03-21, Last modification date: 2012-11-21)

Primary citation

Zhang, H.,Gao, Z.Q.,Wang, W.J.,Liu, G.F.,Shtykova, E.V.,Xu, J.H.,Li, L.F.,Su, X.D.,Dong, Y.H.
The crystal structure of the MPN domain from the COP9 signalosome subunit CSN6
Febs Lett., 586:1147-1153, 2012

PubMed Abstract: The 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 2.5Å 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.

PubMed: 22575649
DOI: 10.1016/j.febslet.2012.03.029

Experimental method

X-RAY DIFFRACTION (2.5 Å)