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Cited by 544

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Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes

Quiocho, Florante A., Ledvina, Polly S.·1996·Molecular Microbiology

Abstract

Summary: Crystallographic structure refinement at very high resolutions of a dozen periplasmic receptors has revealed that, though they have different sizes (26 to 60kDa) and little sequence homology, they have high tertiary structure similarity. They consist of two distinct globular domains bisected by a cleft or groove wherein the ligand binds and is buried by a hinge‐bending motion between the two domains. Structural analysis also reveals how hydrogen‐bonding interactions can be tailored to a wide spectrum of specificity, ranging from the stringent specificity for phosphate and sulphate to the more loose specificity for peptides.

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Crossref · 10.1111/j.1365-2958.1996.tb02484.x

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Metadata

Authors
Quiocho, F. A., & Ledvina, P. S.
Venue
Molecular Microbiology
Publisher
Wiley
Published
1996-04
Volume
20
Issue
1
Pages
17-25
ISSN
  • 0950-382X (ISSN-L)
  • 1365-2958
OpenAlex
W2055956723
Cited by
544
References
0
FWCI
8.02
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes. https://app.cochat.ai/papers/10.1111/j.1365-2958.1996.tb02484.x
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Quiocho, F. A., & Ledvina, P. S. (1996). Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes. Molecular Microbiology. https://doi.org/10.1111/j.1365-2958.1996.tb02484.x

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.