1YO5

Analysis of the 2.0A crystal structure of the protein-DNA complex of human PDEF Ets domain bound to the prostate specific antigen regulatory site

Summary for 1YO5

• Entry DOI: 10.2210/pdb1yo5/pdb
• Descriptor: Enhancer site of Prostate Specific Antigen Promoter Region, SAM pointed domain containing ets transcription factor, ... (4 entities in total)
• Functional Keywords: ets; protein-dna complex; double helix, transcription-dna complex, transcription/dna
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus (Probable): O95238
• Total number of polymer chains: 3
• Total formula weight: 19529.81

Authors

Wang, Y.,Feng, L.,Said, M.,Balderman, S.,Fayazi, Z.,Liu, Y.,Ghosh, D.,Gulick, A.M. (deposition date: 2005-01-26, release date: 2005-05-17, Last modification date: 2023-08-23)

Primary citation

Wang, Y.,Feng, L.,Said, M.,Balderman, S.,Fayazi, Z.,Liu, Y.,Ghosh, D.,Gulick, A.M.
Analysis of the 2.0 A Crystal Structure of the Protein-DNA Complex of the Human PDEF Ets Domain Bound to the Prostate Specific Antigen Regulatory Site
Biochemistry, 44:7095-7106, 2005

PubMed Abstract: PDEF, a prostate epithelial specific transcription factor, is a member of the Ets family of DNA binding proteins. Here we report a 2.0 A crystal structure of the PDEF Ets domain in complex with a natural, high-affinity DNA binding site in the promoter/enhancer region of the human prostate specific antigen gene. Comparison of the PDEF-DNA complex with other Ets complexes revealed key features that are shared among Ets members, as well as important differences in substrate specification at both the "GGA" core and the flanking regions of the DNA site. The combination of the serine residue at position 308 and the glutamine at position 311 explains the previous observation that the PDEF binds preferentially to a thymine at the +4 position of its binding site. Despite the common essential features that are shared among Ets members, PDEF demonstrates distinct patterns of interactions at different positions of DNA in achieving sequence specific recognition. Collectively, the common and unique interactions with both the DNA bases and the backbone phosphates lead to substrate specificity and individual preference for certain DNA sites.

PubMed: 15882048
DOI: 10.1021/bi047352t

Experimental method

X-RAY DIFFRACTION (2 Å)