5g49

Crystal structure of the Arabodopsis thaliana histone-fold dimer L1L NF-YC3

spinqualitylabelsall models 5g49, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5g49 is a 2 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: ACT, CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NFYB6_ARATH Component of the NF-Y/HAP transcription factor complex. The NF-Y complex stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters. Plays a role in the regulation of the embryogenesis. Involved in the abscisic acid (ABA) signaling pathway. Publication Abstract from PubMed The structural analysis of the L1L/NF-YC3 histone dimer from A. thaliana shows that it can trimerize and bind to the CCAAT box. Specific sequence and structural features at the protein/DNA interface, in particular the presence of a Asp-His pair, help explain the molecular mechanisms of LEC1/L1L activity as a bona fide mammalian-like NF-YB. Crystal structure of the Arabidopsis thaliana L1L/NF-YC3 histone-fold dimer reveals specificities of the LEC1 family of NF-Y subunits in plants.,Gnesutta N, Saad D, Chaves-Sanjuan A, Mantovani R, Nardini M Mol Plant. 2016 Nov 18. pii: S1674-2052(16)30276-3. doi:, 10.1016/j.molp.2016.11.006. PMID:27871811 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Nuclear transcription factor Y

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