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Alexander Koglin
Researcher at Los Alamos National Laboratory
Publications - 23
Citations - 1360
Alexander Koglin is an academic researcher from Los Alamos National Laboratory. The author has contributed to research in topics: Protein structure & Membrane protein. The author has an hindex of 16, co-authored 23 publications receiving 1284 citations. Previous affiliations of Alexander Koglin include Harvard University & Goethe University Frankfurt.
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Chlorination by a long-lived intermediate in the mechanism of flavin-dependent halogenases.
TL;DR: This work demonstrates the formation of a long-lived chlorinating intermediate when RebH, FADH2, Cl-, and O2 react in the absence of substrate tryptophan and proposes a Lys-epsilonNH-Cl (lysine chloramine) from reaction of enzyme-generated HOCl with the active site Lys79.
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Structural insights into nonribosomal peptide enzymatic assembly lines
TL;DR: Recent breakthrough achievements in both X-ray and NMR spectroscopic studies are reviewed that illuminate the architecture of NRPS PCP domains, PCP-containing didomain-fragments and of a full termination module (C-A-PCP-TE).
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Conformational Switches Modulate Protein Interactions in Peptide Antibiotic Synthetases
Alexander Koglin,Mohammad Reza Mofid,Frank Löhr,Birgit Schäfer,Vladimir V. Rogov,Marc-Michael Blum,Tanja Mittag,Mohamed A. Marahiel,Frank Bernhard,Volker Dötsch +9 more
TL;DR: This work describes the different states of a peptidyl carrier protein (PCP) that play a crucial role in its function as a peptide shuttle in the nonribosomal peptide synthetases of the tyrocidine A system.
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Dynamic thiolation–thioesterase structure of a non-ribosomal peptide synthetase
Dominique P. Frueh,Haribabu Arthanari,Alexander Koglin,David A. Vosburg,David A. Vosburg,Andrew E. Bennett,Christopher T. Walsh,Gerhard Wagner +7 more
TL;DR: The T–TE interaction described here provides a model for NRPS, PKS and FAS function in general as T– TE-like di-domains typically catalyse the last step in numerous assembly-line chain-termination machineries.
Journal ArticleDOI
Structural basis for the selectivity of the external thioesterase of the surfactin synthetase
Alexander Koglin,Alexander Koglin,Frank Löhr,Frank Bernhard,Vladimir V. Rogov,Dominique P. Frueh,Eric R. Strieter,Mohammad Reza Mofid,Peter Güntert,Peter Güntert,Gerhard Wagner,Christopher T. Walsh,Mohamed A. Marahiel,Volker Dötsch +13 more
TL;DR: The three-dimensional structure of a type II thioesterase from Bacillus subtilis free and in complex with a T domain is reported and it is shown that the TEII enzyme exists in several conformations of which only one is selected on interaction with its native substrate, a modified holo-T domain.