Publications

2023

Andriianov A, Trigüis S, Drobiazko A, Sierro N, Ivanov NV,  Selmer M, Severinov K, Isaev A (2023), "Phage T3 overcomes the BREX defence through SAM cleavage and inhibition of SAM synthesis", bioRxiv doi: https://doi.org/10.1101/2023.02.27.530186
preprint

2022

Larsson DSD, Kanchugal P S & Selmer M (2022), “Structural consequences of deproteinating the 50S ribosome”, Biomolecules 12, 1605 doi: 10.3390/biom12111605
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2021

Brewster JL,  Pachl P, McKellar JLO, Selmer M, Squire CJ & Patrick WM (2021), “Structures and kinetics of Thermotoga maritima MetY reveal new insights into the predominant sulfurylation enzyme of bacterial methionine biosynthesis”, J Biol Chem 296:100797 doi: 10.1016/j.jbc.2021.100797
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Guo X,  Söderholm A, Kanchugal P S, Isaksen GV, Warsi O, Eckhard U, Trigüis S, Gogoll A, Jerlström-Hultqvist J, Åqvist J, Andersson DI & Selmer M (2021), “Structure and mechanism of a phage-encoded SAM lyase revises catalytic function of enzyme family”, eLife 10:e61818. doi: 10.7554/eLife.61818.
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2020

Gustafsson R, Eckhard U, Ye W, Enbody ED, Pettersson M, Jemth P, Andersson L, Selmer M (2020) "Structure and Characterization of Phosphoglucomutase 5 from Atlantic and Baltic Herring-An Inactive Enzyme with Intact Substrate Binding", Biomolecules 10(12):E1631. doi: 10.3390/biom10121631.
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Söderholm A, Newton M S, Patrick W M & Selmer M (2020), “Structure and kinetics of indole-3-glycerol phosphate synthase from Pseudomonas aeruginosa - decarboxylation is not essential for indole formation”, J Biol Chem 295(47):15948-15956. doi: 10.1074/jbc.RA120.014936.
pubmed pdf

Kanchugal P S & Selmer M (2020), “Structural Recognition of Spectinomycin by Resistance Enzyme ANT(9) from Enterococcus faecalis”, Antimicrob Agents Chemother May 21;64(6):e00371-20. doi: May 21;64(6):e00371-20.
pubmed paper  bioRxiv preprint 

Durall C, Kanchugal P S, Selmer M & Lindblad P (2020), “Oligomerization and characteristics of phosphoenolpyruvate carboxylase in Synechococcus PCC 7002” , Sci Rep Feb 27; 10:3607. doi: 10.1038/s41598-020-60249-2.
pubmed

2019

Stsiapanava A, Selmer M (2019), “Crystal structure of ErmE - 23S rRNA methyltransferase in macrolide resistance”, Sci Rep Oct 10; 9(1):14607. doi: 10.1038/s41598-019-51174-0.
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2018

Stern AL*, Van der Verren SE*, Kanchugal P S*, Näsvall J, Gutierrez de Teran H, Selmer M (2018), “Structural mechanism of AadA, a dual specificity aminoglycoside adenylyl transferase from Salmonella enterica”, J Biol Chem doi: 10.1074/jbc.RA118.003989.
*These authors contributed equally
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Jerlström Hultqvist J, Warsi O, Söderholm A, Knopp M, Eckhard U, Vorontsov E, Selmer M, Andersson DI. (2018), “A bacteriophage enzyme induces bacterial metabolic perturbation that confers a novel promiscuous function”, Nat Ecol Evol Aug;2(8):1321-1330. doi: 10.1038/s41559-018-0568-5.
pubmed full text

2017

Newton MS, Guo X, Söderholm A, Näsvall J, Lundström P, Andersson DI, Selmer M, Patrick WM. (2017) "Structural and functional innovations in the real-time evolution of new (βα)₈ barrel enzymes." Proc Natl Acad Sci U S A 114(18):4727-4732. doi: 10.1073/pnas.1618552114. 
pubmed full text

2016

2015

2014

Sun S., Selmer M., Andersson D.I. (2014), “Resistance to β-lactam antibiotics conferred by point mutations in penicillin-binding proteins PBP3, PBP4 and PBP6 in Salmonella enterica.”, PLoS One 9(5):e97202. doi: 10.1371/journal.pone.0097202. eCollection 2014.
pubmed full text

2013

Punekar A.S. & Selmer M. (2013), “Purification, crystallization and preliminary X-ray diffraction analysis of the 23S rRNA methyltransferase RlmJ from Escherichia coli” Acta Cryst. F 69, 1001-1003 
pubmed full text

Punekar A.S., Liljeruhm J., Shepherd T.R., Forster A.C. & Selmer M. (2013), “Structural and functional insights into the molecular mechanism of rRNA m6A methyltransferase RlmJ”, Nucleic Acids Research. 41(20):9537-48. doi: 10.1093/nar/gkt719.
pubmed full text

Hultqvist G, Haq SR, Punekar AS, Chi CN, Engström A, Bach A, Strømgaard K, Selmer M, Gianni S, Jemth P. (2013), “Energetic Pathway Sampling in a Protein Interaction Domain.”, Structure doi:pii: S0969-2126(13)00192-5. 10.1016/j.str.2013.05.010. Epub ahead of print
pubmed full text

2012

Hultqvist G., Punekar A.S., Morrone A., Chi C.N., Engström Å., Selmer M., Gianni S. & Jemth P. (2012), “Tolerance of Protein Folding to a Circular Permutation in a PDZ Domain”, PLOS One. 7(11): 50055. doi:10.1371/journal.pone.0050055
pubmed

Punekar A.S., Shepherd T.R., Liljeruhm J., Forster A.C. & Selmer M. (2012), “Crystal structure of RlmM, the 2′O-ribose methyltransferase for C2498 of Escherichia coli 23S rRNA”, Nucleic Acids Research. 40(20):10507-20. doi: 10.1093/nar/gks727. 
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Koripella R.K., Chen Y., Peisker K., Koh C.S., Selmer M. & Sanyal S. (2012), “Mechanism of elongation factor-G mediated fusidic acid resistance and fitness compensation in Staphylococcus aureus”, J. Biol. Chem. 287(36):30257-67.
pubmed pdf 

Selmer M., Gao Y.G., Weixlbaumer A. & Ramakrishnan V. (2012), “Ribosome engineering to promote new crystal forms”, Acta Cryst. D 68:578-583
pubmed full text

Guo, X., Peisker, K., Bäckbro, K., Chen, Y., Kiran Koripella, R., Mandava, C.S., Sanyal, S. & Selmer, M. (2012), “Structure and function of FusB: an elongation factor G-binding fusidic acid resistance protein active in ribosomal translocation and recycling”, Open Biol., 2: 120016
pubmed full text

2010

Chen, Y., Kiran Koripella, R., Sanyal, S. and Selmer, M. (2010), “Staphylococcus aureus elongation factor G – structure and analysis of a target for fusidic acid”, FEBS J., 277(18):3789-803
pubmed

Haq S.R., Jürgens M.C., Chi C.N., Koh C.S., Elfström L., Selmer M., Gianni S., Jemth P. (2010), "The plastic energy landscape of protein folding: a triangular folding mechanism with an equilibrium intermediate for a small protein domain", J. Biol. Chem., 285(23):18051-9
pubmed

2009

Gao Y.G., Selmer M., Dunham C.M., Weixlbaumer A., Kelley A.C. and Ramakrishnan V. (2009), "The structure of the ribosome with elongation factor G trapped in the posttranslocational state", Science, 326(5953):694-9
pubmed

2008

Selmer, M. and Liljas A. (2008), "Exit biology: battle for the nascent chain", Structure 16:498-500 (preview)
pubmed

2007

Dunham, C.M.*, Selmer, M.*, Phelps, S., Kelley, A.C., Suzuki, T., Joseph, S. and Ramakrishnan, V. (2007), “Structures of tRNAs with an expanded anticodon loop in the decoding center of the 30S Ribosomal Subunit”, RNA, 13(6):817-23, Epub April 6 2007
*These authors contributed equally
pubmed

Weixlbaumer A., Petry, S.^#, Dunham, C.M.^#, Selmer, M.^#, Kelley, A.C. and Ramakrishnan V. (2007), “Crystal structure of the ribosome recycling factor bound to the ribosome”, Nature Struct. Mol. Biol., 14(8): 733-737, Epub July 29 2007; doi:10.1038/nsmb1282
^#These authors contributed equally
pubmed

2006

Selmer, M.*, Dunham, C.M.*, Murphy, F.V. IV, Weixlbaumer, A., Petry, S., Kelley, A.C., Weir, J.R. and Ramakrishnan, V. (2006), “Structure of the 70S ribosome complexed with mRNA and tRNA”, Science, Published online September 7 2006; 10.1126/science.1131127
*These authors contributed equally
pubmed

2005

Petry, S., Brodersen, D.E., Murphy, F.V. IV, Dunham, C.M., Selmer, M., Tarry, M.J., Kelley, A.C. and Ramakrishnan, V. (2005), “Crystal structures of the ribosome in complex with release factors RF1 and RF2 bound to a cognate stop codon”, Cell 123:1255–1266
pubmed

2004

Laurberg, M., Kristensen, O., Selmer, M., Su, X.-D. and Liljas, A. 2004. How do translation factors catalyze protein synthesis. In R. Holland Cheng & Lena Hammar, Eds "Conformational proteomics of Macromolecular Architecture" World Publishing Co. Pte. Ltd. Singapore. Chapter 14, pp307-329.

2003

Nikulin, A., Eliseikina, E., Tishchenko, S., Nevskaya, N., Davydova, N., Platonova, O., Piendl, W., Selmer, M., Liljas, A., Drygin, D., Zimmermann, R., Garber, M. and Nikonov, S. (2003), “Structure of the L1 protuberance in the ribosome”, Nature Struct. Biol. 10(2):104-108
pubmed

2002

Selmer, M., Wilting, R., Holmlund, D. and Su, X-D. (2002), “Preparation of a crystallizable mRNA binding domain of Moorella thermoacetica elongation factor SelB”, Acta Cryst D 58:1871-1873
pubmed

Selmer, M. and Su, X-D. (2002), “Crystal structure of an mRNA binding fragment of Moorella thermoacetica elongation factor SelB”, EMBO J. 41:4145-4153
pubmed

Hirokawa, G., Kiel, M.C., Muto, A., Selmer, M., Liljas, A., Igarashi, K. and Kaji, A. (2002), “Release of tRNA and mRNA from the post-termination complex by Elongation Factor G and Ribosome Recycling Factor, a functional tRNA mimic", EMBO J. 21:2272-2281
pubmed

Selmer, M. (2002) “Protein-RNA interplay in translation. Structural studies of RRF, SelB and L1.” doctoral thesis, Lund University
summary

Kristensen, O., Laurberg, M., Liljas, A. and Selmer, M. (2002), ”Is tRNA mimicry or tRNA binding mandatory for translation factors?”, Curr. Prot. Pept. Sci. 3:133-141 (review)
pubmed

2001

Fedorov, R., Meshcheryakov,V., Gongadze, G., Fomenkova, N., Nevskaya, N., Selmer, M., Laurberg, M., Kristensen, O., Al Karadaghi, S., Liljas, A., Garber, M. and Nikonov, S. (2001) “Structure of ribosomal protein TL5 complexed with RNA provides new insights into the CTC family of stress proteins”, Acta Cryst. D 57:968-976
pubmed

1999

Selmer, M., Al-Karadaghi, S., Hirokawa, G., Kaji, A. and Liljas, A. (1999) “Crystallization and preliminary X-ray analysis of Thermatoga maritima Ribosome Recycling factor”, Acta Cryst. D 55:2049-2050
pubmed

Selmer, M., Al-Karadaghi, S., Hirokawa, G., Kaji, A. and Liljas, A. (1999) “Crystal structure of Thermotoga maritima Ribosome recycling factor: a tRNA mimic”, Science 286:2349-2352
pubmed