4QTK

Complex of WOPR domain of Wor1 in Candida albicans with the 17bp dsDNA

Summary for 4QTK

• Entry DOI: 10.2210/pdb4qtk/pdb
• Related: 4QTJ
• Descriptor: White-opaque regulator 1, DNA (5'-D(*TP*CP*AP*AP*AP*AP*AP*AP*GP*TP*TP*TP*AP*AP*CP*TP*T)-3'), DNA (5'-D(*AP*AP*GP*TP*TP*AP*AP*AP*CP*TP*TP*TP*TP*TP*TP*GP*A)-3'), ... (4 entities in total)
• Functional Keywords: wor1, wopr domain, white-opaque switching, protein-dna recognition, transcriptional regulation, dna binding domain, transcription-dna complex, transcription/dna
• Biological source: Candida albicans SC5314 (Yeast)
• Cellular location: Nucleus : Q5AP80
• Total number of polymer chains: 6
• Total formula weight: 82455.14

Authors

Zhang, S.,Zhang, T.,Ding, J. (deposition date: 2014-07-08, release date: 2014-08-13, Last modification date: 2024-05-29)

Primary citation

Zhang, S.,Zhang, T.,Yan, M.,Ding, J.,Chen, J.
Crystal structure of the WOPR-DNA complex and implications for Wor1 function in white-opaque switching of Candida albicans.
Cell Res., 24:1108-1120, 2014

PubMed Abstract: Wor1 (white-opaque switching regulator 1) is a master regulator of the white-opaque switching in Candida albicans, an opportunistic human fungal pathogen, and is associated with its pathogenicity and commensality. Wor1 contains a conserved DNA-binding region at the N-terminus, consisting of two conserved segments (WOPRa and WOPRb) connected by a non-conserved linker that can bind to specific DNA sequences of the promoter regions and then regulates the transcription. Here, we report the crystal structure of the C. albicans Wor1 WOPR segments in complex with a double-stranded DNA corresponding to one promoter region of WOR1. The sequentially separated WOPRa and WOPRb are structurally interwound together to form a compact globular domain that we term the WOPR domain. The WOPR domain represents a new conserved fungal-specific DNA-binding domain which uses primarily a conserved loop to recognize and interact specifically with a conserved 6-bp motif of the DNA in both minor and major grooves. The protein-DNA interactions are essential for WOR1 transcriptional regulation and white-to-opaque switching. The structural and biological data together reveal the molecular basis for the recognition and binding specificity of the WOPR domain with its specific DNA sequences and the function of Wor1 in the activation of transcription.

PubMed: 25091450
DOI: 10.1038/cr.2014.102

Experimental method

X-RAY DIFFRACTION (2.99 Å)