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  Crystal structure of methylenetetrahydromethanopterin (Mer) in complex with coenzyme F420: Architecture of the F420/FMN binding site of enzymes within the nonprolyl cis-peptide containing bacterial luciferase family

Aufhammer, S. W., Warkentin, E., Ermler, U., Hagemeier, C. H., Thauer, R. K., & Shima, S. (2005). Crystal structure of methylenetetrahydromethanopterin (Mer) in complex with coenzyme F420: Architecture of the F420/FMN binding site of enzymes within the nonprolyl cis-peptide containing bacterial luciferase family. Protein Science, 14(7), 1840-1849. doi:10.1110/ps.041289805.

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 Creators:
Aufhammer, Stephan W.1, 2, Author              
Warkentin, Eberhard3, Author              
Ermler, Ulrich3, Author              
Hagemeier, Christoph H.2, 4, Author
Thauer, Rudolf K.2, 4, Author
Shima, Seigo2, 4, Author
Affiliations:
1Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266277              
2Fachbereich Biologie, Philipps‐Universität, D‐35043 Marburg, Germany, ou_persistent22              
3Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
4Max‐Planck‐Institut für terrestrische Mikrobiologie, D‐35043 Marburg, Germany, ou_persistent22              

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Free keywords: Methylenetetrahydromethanopterin reductase; bacterial luciferase; crystal structure; non-prolyl cis-peptide bond coenzyme F 420; FMN
 Abstract: Methylenetetratetrahydromethanopterin reductase (Mer) is involved in CO2 reduction to methane in methanogenic archaea and catalyses the reversible reduction of methylenetetrahydromethanopterin (methylene-H4MPT) to methyl-H4MPT with coenzyme F(420)H2, which is a reduced 5'-deazaflavin. Mer was recently established as a TIM barrel structure containing a nonprolyl cis-peptide bond but the binding site of the substrates remained elusive. We report here on the crystal structure of Mer in complex with F420 at 2.6 A resolution. The isoalloxazine ring is present in a pronounced butterfly conformation, being induced from the Re-face of F420 by a bulge that contains the non-prolyl cis-peptide bond. The bindingmode of F420 is very similar to that in F420-dependent alcohol dehydrogenase Adf despite the low sequence identity of 21%. Moreover, binding of F420 to the apoenzyme was only associated with minor conformational changes of the polypeptide chain. These findings allowed us to build an improved model of FMN into its binding site in bacterial luciferase, which belongs to the same structural family as Mer and Adf and also contains a nonprolyl cis-peptide bond in an equivalent position.

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Language(s): eng - English
 Dates: 2004-03-222004-12-162004-03-252009-01-012005-07-01
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1110/ps.041289805
PMID: 15937276
PMC: PMC2253363
 Degree: -

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Title: Protein Science
Source Genre: Journal
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Publ. Info: New York, N.Y. : Cambridge University Press
Pages: - Volume / Issue: 14 (7) Sequence Number: - Start / End Page: 1840 - 1849 Identifier: ISSN: 0961-8368
CoNE: https://pure.mpg.de/cone/journals/resource/954925342760