L
Lutz Schmitt
Researcher at University of Düsseldorf
Publications - 202
Citations - 7303
Lutz Schmitt is an academic researcher from University of Düsseldorf. The author has contributed to research in topics: ATP-binding cassette transporter & Secretion. The author has an hindex of 42, co-authored 182 publications receiving 6144 citations. Previous affiliations of Lutz Schmitt include University of Paris & University of Marburg.
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Journal ArticleDOI
A structural classification of substrate-binding proteins
TL;DR: This work proposes a new classification into six clusters of substrate‐binding proteins, based on features of their three‐dimensional structure, and divides these proteins into three structural classes and two functional classes.
Journal ArticleDOI
H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB
TL;DR: The hypothesis that substrate‐assisted catalysis, rather than general base catalysis might operate in ABC‐ATPases is discussed, based on biochemical experiments, and proposed model in which E631 and H662, highly conserved among ABC transporters, form a catalytic dyad.
Journal ArticleDOI
New developments in RiPP discovery, enzymology and engineering
Manuel Montalbán-López,Thomas A Scott,Sangeetha Ramesh,Imran R Rahman,Auke J. van Heel,Jakob H Viel,Vahe Bandarian,Elke Dittmann,Olga Genilloud,Yuki Goto,María José Grande Burgos,Colin Hill,Seokhee Kim,Jesko Koehnke,John A. Latham,A. James Link,Beatriz Martínez,Satish K. Nair,Yvain Nicolet,Sylvie Rebuffat,Hans-Georg Sahl,Dipti Sareen,Eric W. Schmidt,Lutz Schmitt,Konstantin Severinov,Roderich D. Süssmuth,Andrew W. Truman,Huan Wang,Jing-Ke Weng,Gilles P. van Wezel,Qi Zhang,Jin Zhong,Jörn Piel,Douglas A. Mitchell,Oscar P. Kuipers,Wilfred A. van der Donk +35 more
TL;DR: The review discusses the new classes of RiPPs that have been discovered, the advances in the understanding of the installation of both primary and secondary post-translational modifications, and the mechanisms by which the enzymes recognize the leader peptides in their substrates.
Journal ArticleDOI
Structure and mechanism of ABC transporters.
Lutz Schmitt,Robert Tampé +1 more
TL;DR: Recently determined structures of full-length ABC transporters and isolated ABC domains have increased the understanding of the functional mechanism of these proteins.
Journal ArticleDOI
Type 1 protein secretion in bacteria, the ABC-transporter dependent pathway (Review)
TL;DR: While recent structural studies of TolC and MFP-like proteins are providing atomic detail of much of the transport path, structural analysis of the HlyB NBD and other ABC ATPases have revealed details of the catalytic cycle within an NBD dimer and a glimpse of how the action of Hly B is coupled to the translocation of HlA.