NIH VideoCast - Structural and Mechanistic Studies of ABC Transporters: Nature's Favorite Pump

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Structural and Mechanistic Studies of ABC Transporters: Nature's Favorite Pump

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Air date:	Wednesday, May 22, 2013, 3:00:00 PM Time displayed is Eastern Time, Washington DC Local
Views:	Total views: 353 (83 Live, 270 On-demand)
Category:	WALS - Wednesday Afternoon Lectures
Runtime:	01:01:12
Closed captioning:	Check box to display CC outside of the video Note: You can drag the captioning window around and resize it
Description:	Wednesday Afternoon Lecture Series ATP-binding cassette (ABC) transporters, with more than 2,000 members identified, constitute one of the largest protein superfamilies. ABC transporters are ubiquitous membrane proteins that import or export molecules across the cellular membrane. They are integral to almost every biological process, and many are medically important. ABC transporters function by alternating between two states, exposing the substrate-binding site to either side of the membrane. The maltose transport system of E. coli has long been the prototype for ABC transporter research. In her talk, Dr. Chen will present the crystal structures of the maltose transporter captured in multiple conformations and discuss the atomic basis of how chemical energy of ATP hydrolysis is converted to mechanical work of substrate translocation.

NLM Title:	Structural and mechanistic studies of ABC transporters : nature's favorite pump / Jue Chen.
Author:	Chen, Jue. National Institutes of Health (U.S.),
Publisher:
Abstract:	(CIT): Wednesday Afternoon Lecture Series ATP-binding cassette (ABC) transporters, with more than 2,000 members identified, constitute one of the largest protein superfamilies. ABC transporters are ubiquitous membrane proteins that import or export molecules across the cellular membrane. They are integral to almost every biological process, and many are medically important. ABC transporters function by alternating between two states, exposing the substrate-binding site to either side of the membrane. The maltose transport system of E. coli has long been the prototype for ABC transporter research. In her talk, Dr. Chen will present the crystal structures of the maltose transporter captured in multiple conformations and discuss the atomic basis of how chemical energy of ATP hydrolysis is converted to mechanical work of substrate translocation.
Subjects:	ATP-Binding Cassette Transporters--physiology ATP-Binding Cassette Transporters--ultrastructure
Publication Types:	Lecture Webcast
NLM Classification:	QU 55.7
NLM ID:	101609792
CIT Live ID:	12332
Permanent link:	https://videocast.nih.gov/watch=12332

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