2LPB

Structure of the complex of the central activation domain of Gcn4 bound to the mediator co-activator domain 1 of Gal11/med15

Replaces:  2KO4

Summary for 2LPB

• Entry DOI: 10.2210/pdb2lpb/pdb
• NMR Information: BMRB: 18244
• Descriptor: Mediator of RNA polymerase II transcription subunit 15, General control protein GCN4 (2 entities in total)
• Functional Keywords: mediator, activator, co-activator, transcription, nucleus, phosphoprotein, transcription regulation, amino acid biosynthesis, dna-binding
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Nucleus: P19659 P03069
• Total number of polymer chains: 2
• Total formula weight: 13473.12

Authors

Brzovic, P.S.,Heikaus, C.C.,Kisselev, L.,Vernon, R.,Herbig, E.,Pacheco, D.,Warfield, L.,Littlefield, P.,Baker, D.,Klevit, R.E.,Hahn, S. (deposition date: 2012-02-07, release date: 2012-02-22, Last modification date: 2024-05-01)

Primary citation

Brzovic, P.S.,Heikaus, C.C.,Kisselev, L.,Vernon, R.,Herbig, E.,Pacheco, D.,Warfield, L.,Littlefield, P.,Baker, D.,Klevit, R.E.,Hahn, S.
The acidic transcription activator Gcn4 binds the mediator subunit Gal11/Med15 using a simple protein interface forming a fuzzy complex.
Mol.Cell, 44:942-953, 2011

PubMed Abstract: The structural basis for binding of the acidic transcription activator Gcn4 and one activator-binding domain of the Mediator subunit Gal11/Med15 was examined by NMR. Gal11 activator-binding domain 1 has a four-helix fold with a small shallow hydrophobic cleft at its center. In the bound complex, eight residues of Gcn4 adopt a helical conformation, allowing three Gcn4 aromatic/aliphatic residues to insert into the Gal11 cleft. The protein-protein interface is dynamic and surprisingly simple, involving only hydrophobic interactions. This allows Gcn4 to bind Gal11 in multiple conformations and orientations, an example of a "fuzzy" complex, where the Gcn4-Gal11 interface cannot be described by a single conformation. Gcn4 uses a similar mechanism to bind two other unrelated activator-binding domains. Functional studies in yeast show the importance of residues at the protein interface, define the minimal requirements for a functional activator, and suggest a mechanism by which activators bind to multiple unrelated targets.

PubMed: 22195967
DOI: 10.1016/j.molcel.2011.11.008

Experimental method

SOLUTION NMR