6jw5

RVD Q* recognizes 5hmC through water-mediated H bonds

spinqualitylabelsall models 6jw5, resolution 2.99Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6jw5 is a 12 chain structure with sequence from Xanthomonas campestris pv. armoraciae and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.99Å Ligands: 5HC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q3ZD72_XANCA Publication Abstract from PubMed Transcription activator-like effectors (TALEs) recognize DNA through repeat-variable diresidues (RVDs), and TALE-DNA interactions are sensitive to DNA modifications. Our previous study deciphered the recognition of 5-methylcytosine (5mC) and 5-hydroxymethylcytosine (5hmC) by TALEs. Here, we report seven crystal structures of TALE-DNA complexes. The 5mC-specific RVD HA recognizes 5mC through van der Waals interactions and exhibits highly similar loop conformation to natural RVDs. The degenerate RVD RG contacts 5mC and 5hmC via van der Waals interactions as well; however, its loop conformation differs significantly. The loop conformations of universal RVD R* and 5hmC-specific RVD Q* are similar to that of RG, while the interactions of R* with C/5mC/5hmC and Q* with 5hmC are mediated by waters. Together, our findings illustrate the molecular basis for the specific recognition of 5mC and 5hmC by multiple noncanonical TALEs and provide insights into the plasticity of the TALE RVD loops. Structural Insights into the Specific Recognition of 5-methylcytosine and 5-hydroxymethylcytosine by TAL Effectors.,Liu L, Zhang Y, Liu M, Wei W, Yi C, Peng J J Mol Biol. 2020 Feb 14;432(4):1035-1047. doi: 10.1016/j.jmb.2019.11.023. Epub, 2019 Dec 19. PMID:31863750 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also TAL effector

Proteopedia Page Contributors and Editors (what is this?)

OCA