6QE5
| Structure of E.coli RlmJ in complex with the natural cofactor product S-adenosyl-homocysteine (SAH) | Descriptor: | Ribosomal RNA large subunit methyltransferase J, S-ADENOSYL-L-HOMOCYSTEINE | Authors: | Oerum, S, Catala, M, Atdjian, C, Brachet, F, Ponchon, L, Barraud, P, Iannazzo, L, Droogmans, L, Braud, E, Etheve-Quelquejeu, M, Tisne, C. | Deposit date: | 2019-01-04 | Release date: | 2019-03-27 | Last modified: | 2024-01-24 | Method: | X-RAY DIFFRACTION (1.61 Å) | Cite: | Bisubstrate analogues as structural tools to investigate m6A methyltransferase active sites. Rna Biol., 16, 2019
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3CW5
| E. coli Initiator tRNA | Descriptor: | Initiator tRNA | Authors: | Barraud, P, Schmitt, E, Mechulam, Y, Dardel, F, Tisne, C. | Deposit date: | 2008-04-21 | Release date: | 2008-09-02 | Last modified: | 2023-08-30 | Method: | X-RAY DIFFRACTION (3.1 Å) | Cite: | A unique conformation of the anticodon stem-loop is associated with the capacity of tRNAfMet to initiate protein synthesis. Nucleic Acids Res., 36, 2008
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3CW6
| E. coli Initiator tRNA | Descriptor: | Initiator tRNA | Authors: | Barraud, P, Schmitt, E, Mechulam, Y, Dardel, F, Tisne, C. | Deposit date: | 2008-04-21 | Release date: | 2008-09-02 | Last modified: | 2024-02-21 | Method: | X-RAY DIFFRACTION (3.3 Å) | Cite: | A unique conformation of the anticodon stem-loop is associated with the capacity of tRNAfMet to initiate protein synthesis. Nucleic Acids Res., 36, 2008
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4JZS
| Crystal structure of the Bacillus subtilis pyrophosphohydrolase BsRppH (E68A mutant) | Descriptor: | 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, dGTP pyrophosphohydrolase | Authors: | Piton, J, Larue, V, Thillier, Y, Dorleans, A, Pellegrini, O, Li de la Sierra-Gallay, I, Vasseur, J.J, Debart, F, Tisne, C, Condon, C. | Deposit date: | 2013-04-03 | Release date: | 2013-05-08 | Last modified: | 2024-02-28 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Bacillus subtilis RNA deprotection enzyme RppH recognizes guanosine in the second position of its substrates. Proc.Natl.Acad.Sci.USA, 110, 2013
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4JZU
| Crystal structure of the Bacillus subtilis pyrophosphohydrolase BsRppH bound to a non-hydrolysable triphosphorylated dinucleotide RNA (pcp-pGpG) - first guanosine residue in guanosine binding pocket | Descriptor: | 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, RNA (5'-R(*(GCP)P*G)-3'), RNA PYROPHOSPHOHYDROLASE | Authors: | Piton, J, Larue, V, Thillier, Y, Dorleans, A, Pellegrini, O, Li de la Sierra-Gallay, I, Vasseur, J.J, Debart, F, Tisne, C, Condon, C. | Deposit date: | 2013-04-03 | Release date: | 2013-05-08 | Last modified: | 2024-04-03 | Method: | X-RAY DIFFRACTION (1.7 Å) | Cite: | Bacillus subtilis RNA deprotection enzyme RppH recognizes guanosine in the second position of its substrates. Proc.Natl.Acad.Sci.USA, 110, 2013
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4JZT
| Crystal structure of the Bacillus subtilis pyrophosphohydrolase BsRppH (E68A mutant) bound to GTP | Descriptor: | GUANOSINE-5'-TRIPHOSPHATE, dGTP pyrophosphohydrolase | Authors: | Piton, J, Larue, V, Thillier, Y, Dorleans, A, Pellegrini, O, Li de la Sierra-Gallay, I, Vasseur, J.J, Debart, F, Tisne, C, Condon, C. | Deposit date: | 2013-04-03 | Release date: | 2013-05-01 | Last modified: | 2024-04-03 | Method: | X-RAY DIFFRACTION (2.9 Å) | Cite: | Bacillus subtilis RNA deprotection enzyme RppH recognizes guanosine in the second position of its substrates. Proc.Natl.Acad.Sci.USA, 110, 2013
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4JZV
| Crystal structure of the Bacillus subtilis pyrophosphohydrolase BsRppH bound to a non-hydrolysable triphosphorylated dinucleotide RNA (pcp-pGpG) - second guanosine residue in guanosine binding pocket | Descriptor: | 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, MAGNESIUM ION, RNA (5'-R(*(GCP)P*G)-3'), ... | Authors: | Piton, J, Larue, V, Thillier, Y, Dorleans, A, Pellegrini, O, Li de la Sierra-Gallay, I, Vasseur, J.J, Debart, F, Tisne, C, Condon, C. | Deposit date: | 2013-04-03 | Release date: | 2013-05-08 | Last modified: | 2024-04-03 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Bacillus subtilis RNA deprotection enzyme RppH recognizes guanosine in the second position of its substrates. Proc.Natl.Acad.Sci.USA, 110, 2013
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