7v4e | pdb_00007v4e

Crystal Structure of VpsR display novel dimeric architecture and c-di-GMP binding: mechanistic implications in oligomerization, ATPase activity and DNA binding.

spinqualitylabelsall models 7v4e, resolution 4.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7v4e is a 2 chain structure with sequence from Vibrio cholerae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 4Å Ligands: C2E, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9KU59_VIBCH Publication Abstract from PubMed VpsR, the master regulator of biofilm formation in Vibrio cholerae, is an atypical NtrC1 type bEBP lacking residues essential for sigma(54)-RNAP binding and REC domain phosphorylation. Moreover, transcription from PvpsL, a promoter of biofilm biosynthesis, has been documented in presence of sigma(70)-RNAP/VpsR/c-di-GMP complex. It was proposed that c-di-GMP and VpsR together form an active transcription complex with sigma(70)-RNAP. However, the impact of c-di-GMP imparted on VpsR that leads to transcription activation with sigma(70)-RNAP remained elusive, largely due to the lack of the structure of VpsR and knowledge about c-di-GMP:VpsR interactions. In this direction we have solved the crystal structure of VpsR(RA), containing REC and AAA(+) domains, in apo, AMPPNP/GMPPNP and c-di-GMP bound states. Structures of VpsR(RA) unveiled distinctive REC domain orientation that leads to a novel dimeric association and noncanonical ATP/GTP binding. Moreover, we have demonstrated that at physiological pH VpsR remains as monomer having no ATPase activity but c-di-GMP imparted cooperativity to convert it to dimer with potent activity. Crystal structure of c-di-GMP:VpsR(RA) complex reveals that c-di-GMP binds near the C-terminal end of AAA(+) domain. Trp quenching studies on VpsR(R), VpsR(A), VpsR(RA), VpsR(AD) with c-di-GMP additionally demonstrated that c-di-GMP could potentially bind VpsR(D). We propose that c-di-GMP mediated tethering of VpsR(D) with VpsR(A) could likely favor generating the specific protein-DNA architecture for transcription activation. Crystal Structure of VpsR Revealed Novel Dimeric Architecture and c-di-GMP Binding Site: Mechanistic Implications in Oligomerization, ATPase Activity and DNA Binding.,Chakrabortty T, Roy Chowdhury S, Ghosh B, Sen U J Mol Biol. 2022 Jan 30;434(2):167354. doi: 10.1016/j.jmb.2021.167354. Epub 2021 , Nov 10. PMID:34774564 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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