1SV0

Crystal Structure Of Yan-SAM/Mae-SAM Complex

Summary for 1SV0

• Entry DOI: 10.2210/pdb1sv0/pdb
• Related: 1SV4
• Descriptor: Ets DNA-binding protein pokkuri, modulator of the activity of Ets CG15085-PA (3 entities in total)
• Functional Keywords: alpha-helix, 3(10) helix, transcription
• Biological source: Drosophila melanogaster (fruit fly); More
• Cellular location: Nucleus: Q01842
• Total number of polymer chains: 4
• Total formula weight: 38773.36

Authors

Qiao, F.,Song, H.,Kim, C.A.,Sawaya, M.R.,Hunter, J.B.,Gingery, M.,Rebay, I.,Courey, A.J.,Bowie, J.U. (deposition date: 2004-03-26, release date: 2004-07-27, Last modification date: 2024-02-14)

Primary citation

Qiao, F.,Song, H.,Kim, C.A.,Sawaya, M.R.,Hunter, J.B.,Gingery, M.,Rebay, I.,Courey, A.J.,Bowie, J.U.
Derepression by depolymerization; structural insights into the regulation of yan by mae.
Cell(Cambridge,Mass.), 118:163-173, 2004

PubMed Abstract: Yan, an ETS family transcriptional repressor, is regulated by receptor tyrosine kinase signaling via the Ras/MAPK pathway. Phosphorylation and downregulation of Yan is facilitated by a protein called Mae. Yan and Mae interact through their SAM domains. We find that repression by Yan requires the formation of a higher order structure mediated by Yan-SAM polymerization. Moreover, a crystal structure of the Yan-SAM/Mae-SAM complex shows that Mae-SAM specifically recognizes a surface on Yan-SAM that is also required for Yan-SAM polymerization. Mae-SAM binds to Yan-SAM with approximately 1000-fold higher affinity than Yan-SAM binds to itself and can effectively depolymerize Yan-SAM. Mutations on Mae that specifically disrupt its SAM domain-dependent interactions with Yan disable the derepression function of Mae in vivo. Depolymerization of Yan by Mae represents a novel mechanism of transcriptional control that sensitizes Yan for regulation by receptor tyrosine kinases.

PubMed: 15260987
DOI: 10.1016/j.cell.2004.07.010

Experimental method

X-RAY DIFFRACTION (2.07 Å)