6lxf | pdb_00006lxf

Aromatic interactions drive the coupled folding and binding of the intrinsically disordered Sesbania mosaic virus VPg protein.

spinqualitylabelsall models 6lxf, 25 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6lxf is a 1 chain structure with sequence from Sesbania mosaic virus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 6m78 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The plant Sesbania mosaic virus [a (+)-ssRNA sobemovirus] VPg protein is intrinsically disordered in solution. For the virus life cycle, the VPg protein is essential for replication and for polyprotein processing that is carried out by a virus-encoded protease. The nuclear magnetic resonance (NMR)-derived tertiary structure of the protease-bound VPg shows it to have a novel tertiary structure with an alpha-beta-beta-beta topology. The quaternary structure of the high-affinity protease-VPg complex ( approximately 27 kDa) has been determined using HADDOCK protocols with NMR (residual dipolar coupling, dihedral angle, and nuclear Overhauser enhancement) restraints and mutagenesis data as inputs. The geometry of the complex is in excellent agreement with long-range orientational restraints such as residual dipolar couplings and ring-current shifts. A "vein" of aromatic residues on the protease surface is pivotal for the folding of VPg via intermolecular edge-to-face pi...pi stacking between Trp(271) and Trp(368) of the protease and VPg, respectively, and for the CH...pi interactions between Leu(361) of VPg and Trp(271) of the protease. The structure of the protease-VPg complex provides a molecular framework for predicting sites of important posttranslational modifications such as RNA linkage and phosphorylation and a better understanding of the coupled folding upon binding of intrinsically disordered proteins. The structural data presented here augment the limited structural data available on viral proteins, given their propensity for structural disorder. Aromatic Interactions Drive the Coupled Folding and Binding of the Intrinsically Disordered Sesbania mosaic Virus VPg Protein.,Dixit K, Karanth NM, Nair S, Kumari K, Chakrabarti KS, Savithri HS, Sarma SP Biochemistry. 2020 Dec 15;59(49):4663-4680. doi: 10.1021/acs.biochem.0c00721., Epub 2020 Dec 3. PMID:33269926 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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