Crystal structure of the Legionella pneumophila Lpg2936 in complex with the cofactor S-adenosyl-L-methionine reveals novel insights into the mechanism of RsmE family methyltransferases-Reference-Cited by-同舟云学术

Crystal structure of the Legionella pneumophila Lpg2936 in complex with the cofactor S-adenosyl-L-methionine reveals novel insights into the mechanism of RsmE family methyltransferases

Published:2017-10-27 Issue:12 Volume:26 Page:2381-2391
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Pinotsis Nikos¹^ORCID,Waksman Gabriel¹²

Affiliation:

1. Department of Biological Sciences; Institute of Structural and Molecular Biology, Birkbeck; London United Kingdom

2. Institute of Structural and Molecular Biology, Division of Biosciences; University College London; London United Kingdom

Funder

ERC

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference29 articles.

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3. Structural and evolutionary bioinformatics of the SPOUT superfamily of methyltransferases;Tkaczuk;BMC Bioinform,2007

4. SPOUT: a class of methyltransferases that includes spoU and trmD RNA methylase superfamilies, and novel superfamilies of predicted prokaryotic RNA methylases;Anantharaman;J Mol Microbiol Biotech,2002

5. The structure of Rv2372c identifies an RsmE-like methyltransferase from Mycobacterium tuberculosis;Kumar;Acta Cryst,2014

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3. Legionellapneumophila induces methylomic changes in ten-eleven translocation to ensure bacterial reproduction in human lung epithelial cells;Journal of Medical Microbiology;2023-03-16

4. Interfering with Autophagy: The Opposing Strategies Deployed by Legionella pneumophila and Coxiella burnetii Effector Proteins;Frontiers in Cellular and Infection Microbiology;2020-11-05

5. Restriction of S-adenosylmethionine conformational freedom by knotted protein binding sites;PLOS Computational Biology;2020-05-26