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1UBD

CO-CRYSTAL STRUCTURE OF HUMAN YY1 ZINC FINGER DOMAIN BOUND TO THE ADENO-ASSOCIATED VIRUS P5 INITIATOR ELEMENT

Summary for 1UBD
Entry DOI10.2210/pdb1ubd/pdb
DescriptorDNA (5'-D(*AP*GP*GP*GP*TP*CP*TP*CP*CP*AP*TP*TP*TP*TP*GP*AP*A P*GP*CP*G)-3'), DNA (5'-D(*CP*GP*CP*TP*TP*CP*AP*AP*AP*AP*TP*GP*GP*AP*GP*AP*C P*CP*CP*T)-3'), PROTEIN (YY1 ZINC FINGER DOMAIN), ... (5 entities in total)
Functional Keywordstranscription initiation, initiator element, yy1, zinc finger protein, dna- protein recognition, complex (transcription regulation-dna), transcription-dna complex, transcription/dna
Biological sourceHomo sapiens (human)
Total number of polymer chains3
Total formula weight26719.07
Authors
Houbaviy, H.B.,Usheva, A.,Shenk, T.,Burley, S.K. (deposition date: 1996-10-04, release date: 1996-12-23, Last modification date: 2024-02-14)
Primary citationHoubaviy, H.B.,Usheva, A.,Shenk, T.,Burley, S.K.
Cocrystal structure of YY1 bound to the adeno-associated virus P5 initiator.
Proc.Natl.Acad.Sci.USA, 93:13577-13582, 1996
Cited by
PubMed Abstract: Ying-Yang 1 protein (YY1) supports specific, unidirectional initiation of messenger RNA production by RNA polymerase II from two adjacent start sites in the adeno-associated virus P5 promoter, a process which is independent of the TATA box-binding protein (TBP). The 2.5-A resolution YY1-initiator element cocrystal structure reveals four zinc fingers recognizing a YY1-binding consensus sequence. Upstream of the transcription start sites protein-DNA contacts involve both strands and downstream they are virtually restricted to the template strand, permitting access to the active center of RNA polymerase II and ensuring specificity and directionality. The observed pattern of protein-DNA contacts also explains YY1 binding to a preformed transcription bubble, and YY1 binding to a DNA/RNA hybrid analog of the P5 promoter region containing a nascent RNA transcript. A model is proposed for YY1-directed, TBP-independent transcription initiation.
PubMed: 8942976
DOI: 10.1073/pnas.93.24.13577
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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数据于2024-11-06公开中

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