5FD3

Structure of Lin54 tesmin domain bound to DNA

Summary for 5FD3

• Entry DOI: 10.2210/pdb5fd3/pdb
• Descriptor: Protein lin-54 homolog, DNA (5'-D(*GP*AP*GP*TP*TP*TP*GP*AP*AP*AP*CP*T)-3'), DNA (5'-D(*CP*AP*GP*TP*TP*TP*CP*AP*AP*AP*CP*TP*C)-3'), ... (5 entities in total)
• Functional Keywords: transcription factor, tesmin domain, transcription-dna complex, transcription/dna
• Biological source: Homo sapiens (Human); More
• Cellular location: Nucleus : Q6MZP7
• Total number of polymer chains: 6
• Total formula weight: 46672.23

Authors

Marceau, A.H.,Felthousen, J.G.,Goetsch, P.D.,Lee, H.,Tripathi, S.M.,Strome, S.,Litovchick, L.,Rubin, S.M. (deposition date: 2015-12-15, release date: 2016-08-03, Last modification date: 2023-09-27)

Primary citation

Marceau, A.H.,Felthousen, J.G.,Goetsch, P.D.,Iness, A.N.,Lee, H.W.,Tripathi, S.M.,Strome, S.,Litovchick, L.,Rubin, S.M.
Structural basis for LIN54 recognition of CHR elements in cell cycle-regulated promoters.
Nat Commun, 7:12301-12301, 2016

PubMed Abstract: The MuvB complex recruits transcription factors to activate or repress genes with cell cycle-dependent expression patterns. MuvB contains the DNA-binding protein LIN54, which directs the complex to promoter cell cycle genes homology region (CHR) elements. Here we characterize the DNA-binding properties of LIN54 and describe the structural basis for recognition of a CHR sequence. We biochemically define the CHR consensus as TTYRAA and determine that two tandem cysteine rich regions are required for high-affinity DNA association. A crystal structure of the LIN54 DNA-binding domain in complex with a CHR sequence reveals that sequence specificity is conferred by two tyrosine residues, which insert into the minor groove of the DNA duplex. We demonstrate that this unique tyrosine-mediated DNA binding is necessary for MuvB recruitment to target promoters. Our results suggest a model in which MuvB binds near transcription start sites and plays a role in positioning downstream nucleosomes.

PubMed: 27465258
DOI: 10.1038/ncomms12301

Experimental method

X-RAY DIFFRACTION (2.42 Å)