4qtj

Complex of WOPR domain of Wor1 in Candida albicans with the 13bp dsDNA

spinqualitylabelsall models 4qtj, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4qtj is a 3 chain structure with sequence from Candida albicans SC5314. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function WOR1_CANAL Master transcriptional regulator of the switch between 2 heritable states, the white and opaque states. These 2 cell types differ in many characteristics, including cell structure, mating competence, and virulence. Each state is heritable for many generations, and switching between states occurs stochastically, at low frequency. WOR1 Binds the intergenic regions upstream of the genes encoding three additional transcriptional regulators of white-opaque switching, CZF1, EFG1, and WOR2. Phenotypic switching from the white to the opaque phase is a necessary step for mating. Plays a role in cell adhesion and pseudohyphal growth. Publication Abstract from PubMed 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.Cell Research advance online publication 5 August 2014; doi:10.1038/cr.2014.102. Crystal structure of the WOPR-DNA complex and implications for Wor1 function in white-opaque switching of Candida albicans.,Zhang S, Zhang T, Yan M, Ding J, Chen J Cell Res. 2014 Aug 5. doi: 10.1038/cr.2014.102. PMID:25091450 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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