C
Chih-Chia Su
Researcher at Case Western Reserve University
Publications - 65
Citations - 2658
Chih-Chia Su is an academic researcher from Case Western Reserve University. The author has contributed to research in topics: Efflux & Periplasmic space. The author has an hindex of 29, co-authored 56 publications receiving 2202 citations. Previous affiliations of Chih-Chia Su include National Taiwan University of Science and Technology & Iowa State University.
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Journal ArticleDOI
Crystal structures of the CusA efflux pump suggest methionine-mediated metal transport
Feng Long,Chih-Chia Su,Michael T. Zimmermann,Scott E. Boyken,Kanagalaghatta R. Rajashankar,Robert L. Jernigan,Edward W. Yu +6 more
TL;DR: The crystal structure indicates that CusA has, in addition to the three-methionine metal-binding site, four methionine pairs—three located in the transmembrane region and one in the periplasmic domain, which directly suggests a plausible pathway for ion export.
Journal ArticleDOI
Crystal structure of the CusBA heavy-metal efflux complex of Escherichia coli
Chih-Chia Su,Feng Long,Michael T. Zimmermann,Kanagalaghatta R. Rajashankar,Robert L. Jernigan,Edward W. Yu +5 more
TL;DR: The co-crystal structure of the CusBA efflux complex is reported, showing that the transporter (or pump) CusA, which is present as a trimer, interacts with six CusB protomers and that the periplasmic domain of CUSA is involved in these interactions.
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Bacterial multidrug efflux transporters.
TL;DR: The current knowledge of individual pump components of the Cus system, a paradigm for efflux machinery, is described and speculation on how RND pumps assemble to fight diverse antimicrobials is speculated.
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Conformation of the AcrB Multidrug Efflux Pump in Mutants of the Putative Proton Relay Pathway
TL;DR: The X-ray structures of four AcrB mutants revealed remarkably similar conformations, which show striking differences from the previously known conformations of the wild-type protein, and it is believed that this new conformation may mimic, at least partially, one of the transient conformational changes of the transporter during the transport cycle.
Journal ArticleDOI
Crystal Structure of the Membrane Fusion Protein CusB from Escherichia coli
Chih-Chia Su,Feng Yang,Feng Long,Deepak Reyon,Mathew D. Routh,Dennis W. Kuo,Adam K. Mokhtari,Jonathan D. Van Ornam,Katherine L. Rabe,Julie A. Hoy,Young Jin Lee,Kanagalaghatta R. Rajashankar,Edward W. Yu +12 more
TL;DR: Novel structural features of an MFP in the resistance-nodulation-division efflux system of E. coli are revealed and direct evidence that this protein specifically interacts with transported substrates is provided.