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PDBsum entry 2n7h
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Structural protein
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PDB id
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2n7h
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PDB id:
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| Name: |
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Structural protein
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Title:
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Hybrid structure of the type 1 pilus of uropathogenic e.Coli
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Structure:
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Fima. Chain: a, b, c, d, e, f. Synonym: fimbrial protein, type-1 fimbrial protein subunit a, type-1 fimbrial protein, a chain. Engineered: yes
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Source:
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Escherichia coli. Organism_taxid: 562. Gene: fima, jw4277, pgd_03541, pila. Expressed in: escherichia coli. Expression_system_taxid: 562.
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NMR struc:
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10 models
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Authors:
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B.Habenstein,A.Loquet,K.Giller,S.Vasa,S.Becker,M.Habeck,A.Lange
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Key ref:
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B.Habenstein
et al.
(2015).
Hybrid Structure of the Type 1 Pilus of Uropathogenic Escherichia coli.
Angew Chem Int Ed Engl,
54,
11691-11695.
PubMed id:
DOI:
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Date:
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11-Sep-15
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Release date:
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23-Sep-15
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Supersedes:
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PROCHECK
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Headers
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References
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P04128
(FIMA1_ECOLI) -
Type-1 fimbrial protein, A chain from Escherichia coli (strain K12)
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Seq:
Struc:
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182 a.a.
159 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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DOI no:
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Angew Chem Int Ed Engl
54:11691-11695
(2015)
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PubMed id:
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Hybrid Structure of the Type 1 Pilus of Uropathogenic Escherichia coli.
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B.Habenstein,
A.Loquet,
S.Hwang,
K.Giller,
S.K.Vasa,
S.Becker,
M.Habeck,
A.Lange.
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ABSTRACT
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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.
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Links
