5WOP

High Resolution Structure of Mutant CA09-PB2cap

Summary for 5WOP

• Entry DOI: 10.2210/pdb5wop/pdb
• Related: 4ENF 5EG7
• Descriptor: Polymerase PB2, GLYCEROL (3 entities in total)
• Functional Keywords: polymerase basic protein 2, transcription, cap-snatching, rna polymerase, influenza, cap-binding domain, structural genomics
• Biological source: Influenza A virus; More
• Total number of polymer chains: 2
• Total formula weight: 36043.79

Authors

Constantinides, A.E.,Gumpper, R.H.,Severin, C.,Luo, M. (deposition date: 2017-08-02, release date: 2017-12-20, Last modification date: 2023-10-04)

Primary citation

Constantinides, A.,Gumpper, R.,Severin, C.,Luo, M.
High-resolution structure of the Influenza A virus PB2cap binding domain illuminates the changes induced by ligand binding.
Acta Crystallogr F Struct Biol Commun, 74:122-127, 2018

PubMed Abstract: In the face of increasing drug resistance and the rapidly increasing necessity for practicality in clinical settings, drugs targeting different viral proteins are needed in order to control influenza A and B. A small molecule that tenaciously adheres to the PB2cap binding domain, part of the heterotrimeric RNA polymerase machinery of influenza A virus and influenza B virus, is a promising drug candidate. Understanding the anatomic behavior of PB2cap upon ligand binding will aid in the development of a more robust inhibitor. In this report, the anatomic behavior of the influenza A virus PB2cap domain is established by solving the crystal structure of native influenza A virus PB2cap at 1.52 Å resolution. By comparing it with the ligand-bound structure, the dissociation and rotation of the ligand-binding domain in PB2cap from the C-terminal domain is identified. This domain movement is present in many PB2cap structures, suggesting its functional relevance for polymerase activity.

PubMed: 29497014
DOI: 10.1107/S2053230X18000894

Experimental method

X-RAY DIFFRACTION (1.52 Å)