High-Affinity E. coli Methionine ABC Transporter: Structure and Allosteric Regulation
High-Affinity E. coli Methionine ABC Transporter: Structure and Allosteric Regulation
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Publisher
Washington, DC: American Association for the Advancement of Science
Journal title
Language
English
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Publisher
Washington, DC: American Association for the Advancement of Science
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Scope and Contents
Contents
The crystal structure of the high-affinity Escherichia coli MetNI methionine uptake transporter, a member of the adenosine triphosphate (ATP)-binding cassette (ABC) family, has been solved to 3.7 angstrom resolution. The overall architecture of MetNI reveals two copies of the adenosine triphosphatase (ATPase) MetN in complex with two copies of the...
Alternative Titles
Full title
High-Affinity E. coli Methionine ABC Transporter: Structure and Allosteric Regulation
Authors, Artists and Contributors
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Record Identifier
TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2527972
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2527972
Other Identifiers
ISSN
0036-8075
E-ISSN
1095-9203
DOI
10.1126/science.1157987
