5mll

Structure of HpDprA at 1.9 Angstroms resolution

spinqualitylabelsall models 5mll, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5mll is a 2 chain structure with sequence from Helicobacter pylori 26695. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: EDO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function O25100_HELPY Publication Abstract from PubMed DprA, a ubiquitous multidomain DNA-binding protein, plays a crucial role during natural transformation in bacteria. Here, we carried out the structural analysis of DprA from the human pathogen Helicobacter pylori by combining data issued from the 1.8 A resolution X-ray structure of the Pfam02481 domain dimer (RF), the NMR structure of the carboxy-terminal domain (CTD) and the low-resolution structure of the full-length DprA dimer obtained in solution by SAXS. In particular, we sought a molecular function for the CTD, a domain that we show here is essential for transformation in H. pylori. Albeit its structural homology to winged helix DNA binding motifs, we confirmed that the isolated CTD does not interact with ssDNA nor with dsDNA. The key R52 and K137 residues of RF are crucial for these two interactions. Search for sequences harboring homology to either HpDprA or Rhodopseudomonas palustris DprA CTDs led to the identification of conserved patches in the two CTD. Our structural study revealed the similarity of the structures adopted by these residues in RpDprA CTD and HpDprA CTD. This argues for a conserved, but yet to be defined, CTD function, distinct from DNA binding. This article is protected by copyright. All rights reserved. The C-terminal domain of HpDprA is a DNA-binding Winged Helix domain that does not bind double-stranded DNA.,Lisboa J, Celma L, Sanchez D, Marquis M, Andreani J, Guerois R, Ochsenbein F, Durand D, Marsin S, Cuniasse P, Radicella JP, Quevillon-Cheruel S FEBS J. 2019 Feb 16. doi: 10.1111/febs.14788. PMID:30771270 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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