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-Structure paper
Title | The TPR domain of PgaA is a multifunctional scaffold that binds PNAG and modulates PgaB-dependent polymer processing. |
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Journal, issue, pages | Plos Pathog., Vol. 18, Page e1010750-e1010750, Year 2022 |
Publish date | Dec 16, 2021 (structure data deposition date) |
![]() | 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. ...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. |
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Methods | X-ray diffraction |
Resolution | 2.85 Å |
Structure data | ![]() PDB-7t8n: |
Chemicals | ![]() ChemComp-MG: ![]() ChemComp-CL: ![]() ChemComp-HOH: |
Source |
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![]() | STRUCTURAL PROTEIN / PNAG binding module / tetra-trico repeat (TPR) domain / PNAG secretion |