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Structure paper

TitleThe TPR domain of PgaA is a multifunctional scaffold that binds PNAG and modulates PgaB-dependent polymer processing.
Journal, issue, pagesPlos Pathog., Vol. 18, Page e1010750-e1010750, Year 2022
Publish dateDec 16, 2021 (structure data deposition date)
AuthorsPfoh, R. / Subramanian, A.S. / Huang, J. / Little, D.J. / Forman, A. / DiFrancesco, B.R. / Balouchestani-Asli, N. / Kitova, E.N. / Klassen, J.S. / Pomes, R. ...Pfoh, R. / Subramanian, A.S. / Huang, J. / Little, D.J. / Forman, A. / DiFrancesco, B.R. / Balouchestani-Asli, N. / Kitova, E.N. / Klassen, J.S. / Pomes, R. / Nitz, M. / Howell, P.L.
External linksPlos Pathog. / PubMed:35930610
MethodsX-ray diffraction
Resolution2.85 Å
Structure data

PDB-7t8n:
Crystal structure of the PNAG binding module PgaA-TPR 220-359
Method: X-RAY DIFFRACTION / Resolution: 2.85 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • escherichia coli k-12 (bacteria)
KeywordsSTRUCTURAL PROTEIN / PNAG binding module / tetra-trico repeat (TPR) domain / PNAG secretion

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