The E. coli BtuCD Structure: A Framework for ABC Transporter Architecture and Mechanism

By K. Locher, Allen T. Lee, D. Rees. Science, 2002

1,061 citations recorded by the source corpus.

Subfields: Molecular Biology, Molecular Medicine, Oncology

View Paper: https://www.semanticscholar.org/paper/c0c89a8a1c80867544fcb22577265bdf4716835f

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. Debora Marks
2. Christopher Sander
3. Lucy J. Colwell
4. Burkhard Rost
5. Thomas A. Hopf
6. David T. Jones
7. Jianlin Cheng
8. Jinbo Xu

In Molecular Medicine

1. E. Dassa
2. C. Orelle
3. K. Locher
4. A. Davidson
5. Jue Chen
6. Yigong Shi
7. S. Wilkens
8. C. Higgins

In Oncology

1. K. Locher
2. E. Dassa
3. C. Orelle
4. A. Davidson
5. Jue Chen
6. S. Wilkens
7. Yigong Shi
8. C. Higgins

Citations in the corpus

• RCSB Protein Data Bank: Enabling biomedical research and drug discovery (2019, background): “Instructive examples include an early structure of the vitamin b12 transporter (BtuCD, PDB 1l7v), 78 and three states of the E. coli maltose transporter MalEFGK2 (inward-open, PDB 3fh6 79 ; pretranslocation, PDB 3pv0 80 ; and outward-open, PDB 2r6g 81 ).”
• Transmembrane transport of endo- and xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins. (2006, background): “Although there is no discernible primary structure homology, the NH2-terminal region of the recently crystallized bacterial vitamin B12 transporter subunit BtuC contains a relatively long -helix (residues 2–32) that appears to be laterally associated with, or embedded in, the inner leaflet of the li”
• The ATP switch model for ABC transporters (2004, background): “structures, and subsequently in the complete BtuCD transporte”
• Overcoming ABC transporter-mediated multidrug resistance: Molecular mechanisms and novel therapeutic drug strategies. (2016, background): “Subsequently, the crystal structure of the vitamin B12 transporter BtuCD from E.coli was determined at a resolution of 3.2 Å (Locher and Borths, 2004; Locher et al., 2002).”
• Mechanistic diversity in ATP-binding cassette (ABC) transporters (2016, methodology): “In bacterial ABC importers, TMDs are expressed as separate protein subunits that either belong to type I or type II based on whether the fold is similar to that first observed in A. fulgidus ModBC 41 (type 1) or E. coli BtuCD 53 (type 2).”
• Structure and mechanism of ABC transporters (2015, background): “coli maltose [22,23] (a type I) and vitamin B12 [24,36,37] (a type II) uptake systems.”