S
Susan K. Buchanan
Researcher at National Institutes of Health
Publications - 98
Citations - 7329
Susan K. Buchanan is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Bacterial outer membrane & Periplasmic space. The author has an hindex of 41, co-authored 95 publications receiving 6483 citations. Previous affiliations of Susan K. Buchanan include Birkbeck, University of London & Laboratory of Molecular Biology.
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Journal ArticleDOI
TonB-Dependent Transporters: Regulation, Structure, and Function
TL;DR: Recent progress in understanding regulation, structure, and function in TBDTs is summarized and questions remaining to be answered are summarized.
Journal ArticleDOI
Crystal structure of the outer membrane active transporter FepA from Escherichia coli.
Susan K. Buchanan,Susan K. Buchanan,Barbara S. Smith,Lalitha Venkatramani,Di Xia,Lothar Esser,Maya Palnitkar,Ranjan Chakraborty,Dick Van der Helm,Johann Deisenhofer +9 more
TL;DR: The blockage of the pore suggests that the N–terminal domain must undergo a conformational rearrangement to allow ligand transport into the periplasm, and this structure could provide a signaling pathway between the processes of ligand recognition and TonB–mediated transport.
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Structural insight into the biogenesis of β-barrel membrane proteins
Nicholas Noinaj,Adam J. Kuszak,James C. Gumbart,Petra Lukacik,Hoshing Chang,Nicole C. Easley,Trevor Lithgow,Susan K. Buchanan +7 more
TL;DR: The structure of BamA is described, the central and essential component of the BAM complex, from two species of bacteria: Neisseria gonorrhoeae and Haemophilus ducreyi, which consists of a large periplasmic domain attached to a 16-strand transmembrane β-barrel domain.
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Crystal structure of the catalytic portion of human HMG‐CoA reductase: insights into regulation of activity and catalysis
TL;DR: The crystal structure of the catalytic portion of human HMGR explains the influence of the enzyme's oligomeric state on the activity and suggests a mechanism for cholesterol sensing.
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Structural basis for iron piracy by pathogenic Neisseria
Nicholas Noinaj,Nicole C. Easley,Muse Oke,Naoko Mizuno,James C. Gumbart,Evzen Boura,Ashley N. Steere,Olga Zak,Philip Aisen,Emad Tajkhorshid,Robert W. Evans,Andrew Gorringe,Anne B. Mason,Alasdair C. Steven,Susan K. Buchanan +14 more
TL;DR: This work solved crystal structures of the TbpA–transferrin complex and of the corresponding co-receptor TbpB and provides a rational basis for the specificity of TBPA for human transferrin, and shows how TBCA promotes iron release from transferrin and elucidate how TBPB facilitates this process.