Structural and dynamical rationale for fatty acid unsaturation in Escherichia coli
Structural and dynamical rationale for fatty acid unsaturation in Escherichia coli
About this item
Full title
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Publisher
United States: National Academy of Sciences
Journal title
Language
English
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Publisher
United States: National Academy of Sciences
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Scope and Contents
Contents
Fatty acid biosynthesis in α- and γ-proteobacteria requires two functionally distinct dehydratases, FabA and FabZ. Here, mechanistic cross-linking facilitates the structural characterization of a stable hexameric complex of six Escherichia coli FabZ dehydratase subunits with six AcpP acyl carrier proteins. The crystal structure sheds light on the d...
Alternative Titles
Full title
Structural and dynamical rationale for fatty acid unsaturation in Escherichia coli
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Record Identifier
TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6452729
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6452729
Other Identifiers
ISSN
0027-8424
E-ISSN
1091-6490
DOI
10.1073/pnas.1818686116
