8ylj | pdb_00008ylj

Crystal structure of Pectobacterium atrosepticum PecS in complex with uric acid

spinqualitylabelsall models 8ylj, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8ylj is a 1 chain structure with sequence from Pectobacterium atrosepticum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.05Å Ligands: URC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q6D5K4_PECAS Publication Abstract from PubMed Uric acid (UA)-responsive transcriptional regulators (UrtRs), which belong to the multiple antibiotic resistance regulator (MarR) superfamily, transcriptionally coordinate virulence and metabolism in bacteria by modulating interactions with operator DNA in response to UA. To elucidate the transcriptional regulatory mechanism of UrtR, we structurally analyzed UrtR proteins, including PecS, MftR, and HucR, alone and in complex with UA or DNA. UrtR contains a dimerization domain (DD) and a winged helix-turn-helix domain (wHTHD) and forms a homodimer primarily via the DD, as observed for other MarR superfamily proteins. However, UrtRs are characterized by a unique N-terminal alpha-helix, which contributes to dimerization and UA recognition. In the absence of UA, the UrtR dimer symmetrically binds to the operator double-stranded DNA (dsDNA) by inserting its alpha4 recognition helix and beta-stranded wing within the wHTHD into the major and minor grooves of dsDNA, respectively. Upon exposure to UA, UrtR accommodates UA in the intersubunit pocket between the DD and wHTHD. UA binding induces a conformational change in the major groove-binding core element of the UrtR wHTHD, generating a DNA binding-incompatible structure. This local allosteric mechanism of UrtR completely differs from that generally observed in other MarR superfamily members, in which the entire wHTHD undergoes effector-responsive global shifts. Structural basis of transcriptional regulation by UrtR in response to uric acid.,Song WS, Ki DU, Cho HY, Kwon OH, Cho H, Yoon SI Nucleic Acids Res. 2024 Nov 27;52(21):13192-13205. doi: 10.1093/nar/gkae922. PMID:39484741 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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