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2N7H

Hybrid structure of the Type 1 Pilus of Uropathogenic E.coli

Replaces:  2MX3
Summary for 2N7H
Entry DOI10.2210/pdb2n7h/pdb
NMR InformationBMRB: 25334
DescriptorFimA (1 entity in total)
Functional Keywordsstructural protein
Biological sourceEscherichia coli
Total number of polymer chains6
Total formula weight95798.64
Authors
Habenstein, B.,Loquet, A.,Giller, K.,Vasa, S.,Becker, S.,Habeck, M.,Lange, A. (deposition date: 2015-09-11, release date: 2015-09-23, Last modification date: 2015-10-14)
Primary citationHabenstein, B.,Loquet, A.,Hwang, S.,Giller, K.,Vasa, S.K.,Becker, S.,Habeck, M.,Lange, A.
Hybrid Structure of the Type 1 Pilus of Uropathogenic Escherichia coli.
Angew.Chem.Int.Ed.Engl., 54:11691-11695, 2015
Cited by
PubMed Abstract: Type 1 pili are filamentous protein assemblies on the surface of Gram-negative bacteria that mediate adhesion to host cells during the infection process. The molecular structure of type 1 pili remains elusive on the atomic scale owing to their insolubility and noncrystallinity. Herein we describe an approach for hybrid-structure determination that is based on data from solution-state NMR spectroscopy on the soluble subunit and solid-state NMR spectroscopy and STEM data on the assembled pilus. Our approach is based on iterative modeling driven by structural information extracted from different sources and provides a general tool to access pseudo atomic structures of protein assemblies with complex subunit folds. By using this methodology, we determined the local conformation of the FimA pilus subunit in the context of the assembled type 1 pilus, determined the exact helical pilus architecture, and elucidated the intermolecular interfaces contributing to pilus assembly and stability with atomic detail.
PubMed: 26267365
DOI: 10.1002/anie.201505065
PDB entries with the same primary citation
Experimental method
SOLID-STATE NMR
Structure validation

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