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crystal-structure (3) 3
glycosylation (3) 3
polyproline stretches (3) 3
microbiology (2) 2
protein biosynthesis (2) 2
pseudomonas aeruginosa (2) 2
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tdp-rhamnose (2) 2
transfer-rna synthetase (2) 2
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amino acid sequence (1) 1
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bacillus-subtilis (1) 1
bacterial proteins (1) 1
bacterial two-hybrid (1) 1
bepress|life sciences|biochemistry, biophysics, and structural biology|biochemistry (1) 1
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factor ef-p (1) 1
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1. Full Text Structural Basis of an Asymmetric Condensin ATPase Cycle
by Hassler, Markus and Shaltiel, Indra A and Kschonsak, Marc and Simon, Bernd and Merkel, Fabian and Thärichen, Lena and Bailey, Henry J and Macošek, Jakub and Bravo, Sol and Metz, Jutta and Hennig, Janosch and Haering, Christian H
Molecular Cell, ISSN 1097-2765, 06/2019, Volume 74, Issue 6, pp. 1175 - 1188.e9
The condensin protein complex plays a key role in the structural organization of genomes. How the ATPase activity of its SMC subunits drives large-scale... 
condensin | cohesin | SMC protein complex | ABC ATPase | genome organization | mitotic chromosome | structural biology | DNA loop extrusion | MOLECULAR-REPLACEMENT | FULLY-AUTOMATIC CHARACTERIZATION | STRUCTURE REFINEMENT | DATA-COLLECTION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | COHESIN RING | CHROMOSOME CONDENSATION | PROTEIN COMPLEXES | CRYSTALLOGRAPHY | DNA EXIT GATE | CELL BIOLOGY | Proteins | Atoms | Genomics | Cells | Adenosine triphosphatase
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2. Full Text Structural basis for EarP-mediated arginine glycosylation of translation elongation factor EF-P
by Krafczyk, Ralph and Macošek, Jakub and Jagtap, Pravin Kumar Ankush and Gast, Daniel and Wunder, Swetlana and Mitra, Prithiba and Jha, Amit Kumar and Rohr, Jürgen and Hoffmann-Röder, Anja and Jung, Kirsten and Hennig, Janosch and Lassak, Jürgen
mBio, ISSN 2161-2129, 09/2017, Volume 8, Issue 5, p. e01412-17
Glycosylation is a universal strategy to posttranslationally modify proteins. The recently discovered arginine rhamnosylation activates the... 
Posttranslational modification | Translation | Glycosyltransferase | Ribosomes | Nucleotide sugar | Pseudomonas aeruginosa | Glycosylation | Pseudomonas putida | TDP-rhamnose | SYSTEM | BIOLOGICAL MACROMOLECULES | posttranslational modification | PROTEIN-STRUCTURE | CRYSTAL-STRUCTURE | ESCHERICHIA-COLI | glycosylation | MICROBIOLOGY | nucleotide sugar | POLYPROLINE STRETCHES | SWISS-MODEL | ribosomes | NMR | TRANSFER-RNA SYNTHETASE | glycosyltransferase | translation | PEPTIDE-BOND | Amino Acid Sequence | Pseudomonas putida - genetics | Peptide Elongation Factors - metabolism | Protein Biosynthesis | Models, Molecular | Pseudomonas putida - enzymology | Bacterial Proteins | Pseudomonas putida - chemistry | Pseudomonas putida - metabolism | Glycosyltransferases - metabolism | Peptide Elongation Factors - chemistry | Pseudomonas aeruginosa - pathogenicity | Ribosomes - genetics | Pseudomonas aeruginosa - enzymology | Pseudomonas aeruginosa - metabolism | Protein Processing, Post-Translational | Glycosyltransferases - genetics | Peptide Elongation Factors - genetics | Arginine - metabolism
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3. Full Text Switching the Post-translational Modification of Translation Elongation Factor EF-P
by Volkwein, Wolfram and Krafczyk, Ralph and Jagtap, Pravin Kumar Ankush and Parr, Marina and Mankina, Elena and Macošek, Jakub and Guo, Zhenghuan and Fürst, Maximilian Josef Ludwig Johannes and Pfab, Miriam and Frishman, Dmitrij and Hennig, Janosch and Jung, Kirsten and Lassak, Jürgen
Frontiers in microbiology, ISSN 1664-302X, 2019, Volume 10, p. 1148
Tripeptides with two consecutive prolines are the shortest and most frequent sequences causing ribosome stalling. The bacterial translation elongation factor P... 
CRYSTAL-STRUCTURE | bacterial two-hybrid | glycosylation | MICROBIOLOGY | IF5A | POLYPROLINE STRETCHES | PROTEIN-SYNTHESIS | TDP-rhamnose | PEPTIDYL-TRANSFER | TRANSFER-RNA SYNTHETASE | BACILLUS-SUBTILIS | Pseudomonas aeruginosa | R PACKAGE | EarP | NIeB | PROMOTES TRANSLATION | PROLINE | EpmA | RIBOSOME | Post-translational modification | Proline | Protein biosynthesis | Lysine | Escherichia coli | Translation elongation factors | Usage | Cladistic analysis | Research | Pseudomonas putida
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4. Full Text Resolving the alpha-glycosidic linkage of arginine-rhamnosylated translation elongation factor P triggers generation of the first Arg(Rha) specific antibody
by Li, X and Krafczyk, R and Macosek, J and Li, YL and Zou, Y and Simon, B and Pan, X and Wu, QY and Yan, F and Li, S and Hennig, J and Jung, K and Lassak, J and Hu, HG
CHEMICAL SCIENCE, ISSN 2041-6520, 2016, Volume 7, Issue 12, pp. 6995 - 7001
A previously discovered posttranslational modification strategy - arginine rhamnosylation - is essential for elongation factor P (EF-P) dependent rescue of... 
FACTOR EF-P | PROTEIN | GLCNACYLATION | PATHWAY | SYNTHETASE | GLYCOSYLATION | GLYCOPEPTIDES | GLYCOSYLTRANSFERASES | POLYPROLINE STRETCHES | CHEMISTRY, MULTIDISCIPLINARY | RIBOSOME
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5. Full Text Resolving the α-glycosidic linkage of arginine-rhamnosylated translation elongation factor P triggers generation of the first ArgRha specific antibody† †Electronic supplementary information (ESI) available: Experimental details and chemical compound characterization. CCDC 1469830. For ESI and crystallographic data in CIF or other electronic format see DOI: 10.1039/c6sc02889f Click here for additional data file. Click here for additional data file
by Li, Xiang and Krafczyk, Ralph and Macošek, Jakub and Li, Yu-Lei and Zou, Yan and Simon, Bernd and Pan, Xing and Wu, Qiu-Ye and Yan, Fang and Li, Shan and Hennig, Janosch and Jung, Kirsten and Lassak, Jürgen and Hu, Hong-Gang
Chemical Science, ISSN 2041-6520, 12/2016, Volume 7, Issue 12, pp. 6995 - 7001
Here we describe a potent tool to investigate arginine rhamnosylation and develop novel antibiotics. A previously discovered posttranslational modification... 
Chemistry
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6. Full Text Resolving the α-glycosidic linkage of arginine-rhamnosylated translation elongation factor P triggers generation of the first Arg Rha specific antibody
by Li, Xiang and Krafczyk, Ralph and Macošek, Jakub and Li, Yu-Lei and Zou, Yan and Simon, Bernd and Pan, Xing and Wu, Qiu-Ye and Yan, Fang and Li, Shan and Hennig, Janosch and Jung, Kirsten and Lassak, Jürgen and Hu, Hong-Gang
Chemical science, ISSN 2041-6520, 12/2016, Volume 7, Issue 12, p. 6995
A previously discovered posttranslational modification strategy - arginine rhamnosylation - is essential for elongation factor P (EF-P) dependent rescue of... 
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7. Full Text Resolving the α-glycosidic linkage of arginine-rhamnosylated translation elongation factor P triggers generation of the first ArgRha specific antibodyElectronic supplementary information (ESI) available: Experimental details and chemical compound characterization. CCDC 1469830. For ESI and crystallographic data in CIF or other electronic format see DOI: 10.1039/c6sc02889f
by Li, Xiang and Krafczyk, Ralph and Macošek, Jakub and Li, Yu-Lei and Zou, Yan and Simon, Bernd and Pan, Xing and Wu, Qiu-Ye and Yan, Fang and Li, Shan and Hennig, Janosch and Jung, Kirsten and Lassak, Jürgen and Hu, Hong-Gang
ISSN 2041-6520, 11/2016, Volume 7, Issue 12, pp. 6995 - 71
A previously discovered posttranslational modification strategy - arginine rhamnosylation - is essential for elongation factor P (EF-P) dependent rescue of... 
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