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RNA polymerase I structure and transcription regulation.
Engel C, Sainsbury S, Cheung AC, Kostrewa D, Cramer P. Engel C, et al. Nature. 2013 Oct 31;502(7473):650-5. doi: 10.1038/nature12712. Epub 2013 Oct 23. Nature. 2013. PMID: 24153182
Mechanisms of backtrack recovery by RNA polymerases I and II.
Lisica A, Engel C, Jahnel M, Roldán É, Galburt EA, Cramer P, Grill SW. Lisica A, et al. Proc Natl Acad Sci U S A. 2016 Mar 15;113(11):2946-51. doi: 10.1073/pnas.1517011113. Epub 2016 Feb 29. Proc Natl Acad Sci U S A. 2016. PMID: 26929337 Free PMC article.
Distinct Mechanisms of Transcription Initiation by RNA Polymerases I and II.
Engel C, Neyer S, Cramer P. Engel C, et al. Annu Rev Biophys. 2018 May 20;47:425-446. doi: 10.1146/annurev-biophys-070317-033058. Annu Rev Biophys. 2018. PMID: 29792819 Review.
Structural Basis of RNA Polymerase I Transcription Initiation.
Engel C, Gubbey T, Neyer S, Sainsbury S, Oberthuer C, Baejen C, Bernecky C, Cramer P. Engel C, et al. Cell. 2017 Mar 23;169(1):120-131.e22. doi: 10.1016/j.cell.2017.03.003. Cell. 2017. PMID: 28340337
Structure of RNA polymerase I transcribing ribosomal DNA genes.
Neyer S, Kunz M, Geiss C, Hantsche M, Hodirnau VV, Seybert A, Engel C, Scheffer MP, Cramer P, Frangakis AS. Neyer S, et al. Nature. 2016 Dec 22;540(7634):607-610. doi: 10.1038/nature20561. Epub 2016 Nov 14. Nature. 2016. PMID: 27842382
RNA polymerase I-Rrn3 complex at 4.8 Å resolution.
Engel C, Plitzko J, Cramer P. Engel C, et al. Nat Commun. 2016 Jul 15;7:12129. doi: 10.1038/ncomms12129. Nat Commun. 2016. PMID: 27418309 Free PMC article.
An alternative RNA polymerase I structure reveals a dimer hinge.
Kostrewa D, Kuhn CD, Engel C, Cramer P. Kostrewa D, et al. Acta Crystallogr D Biol Crystallogr. 2015 Sep;71(Pt 9):1850-5. doi: 10.1107/S1399004715012651. Epub 2015 Aug 25. Acta Crystallogr D Biol Crystallogr. 2015. PMID: 26327374
The recent crystal structure of Pol I at 2.8 Å resolution revealed two novel elements: the `expander' in the active-centre cleft and the `connector' that mediates Pol I dimerization [Engel et al. (2013), Nature (London), 502, 650-655]. ...
The recent crystal structure of Pol I at 2.8 Å resolution revealed two novel elements: the `expander' in the active-centre cleft and the `co …
The 1.8 A crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: implications for substrate binding and reaction mechanism.
Mathieu M, Modis Y, Zeelen JP, Engel CK, Abagyan RA, Ahlberg A, Rasmussen B, Lamzin VS, Kunau WH, Wierenga RK. Mathieu M, et al. J Mol Biol. 1997 Oct 31;273(3):714-28. doi: 10.1006/jmbi.1997.1331. J Mol Biol. 1997. PMID: 9402066
The central helix in the C-terminal domain exposes its polar residues to an interior polar pocket. The refined structure has also been used to predict the mode of binding of the substrate molecule acetoacetyl-CoA, as well as the reaction mechanism. ...
The central helix in the C-terminal domain exposes its polar residues to an interior polar pocket. The refined structure has also bee …
FlhA provides the adaptor for coordinated delivery of late flagella building blocks to the type III secretion system.
Bange G, Kümmerer N, Engel C, Bozkurt G, Wild K, Sinning I. Bange G, et al. Proc Natl Acad Sci U S A. 2010 Jun 22;107(25):11295-300. doi: 10.1073/pnas.1001383107. Epub 2010 Jun 2. Proc Natl Acad Sci U S A. 2010. PMID: 20534509 Free PMC article.
The major filament protein (flagellin) and the filament-cap protein (FliD) bind to the FlhA cytoplasmic domain (FlhA-C) only in complex with their cognate chaperones (FliS and FliT). To understand the molecular details of these interactions we determined the FlhA-C …
The major filament protein (flagellin) and the filament-cap protein (FliD) bind to the FlhA cytoplasmic domain (FlhA-C) only in compl …
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