6BI6
 
 | | Solution NMR structure of uncharacterized protein YejG | | Descriptor: | Uncharacterized protein YejG | | Authors: | Mohanty, B, Finn, T.J, Macindoe, I, Zhong, J, Patrick, W.M, Mackay, J.P. | | Deposit date: | 2017-11-01 | | Release date: | 2018-11-07 | | Last modified: | 2024-05-15 | | Method: | SOLUTION NMR | | Cite: | The uncharacterized bacterial protein YejG has the same architecture as domain III of elongation factor G.
Proteins, 87, 2019
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5G4Z
 | | Structural basis for carboxylic acid recognition by a Cache chemosensory domain. | | Descriptor: | Methyl-accepting chemotaxis sensory transducer with Cache sensor, TRIETHYLENE GLYCOL, UNKNOWN LIGAND | | Authors: | Brewster, J, McKellar, J.L.O, Newman, J, Peat, T.S, Gerth, M.L. | | Deposit date: | 2016-05-18 | | Release date: | 2017-03-29 | | Last modified: | 2024-01-10 | | Method: | X-RAY DIFFRACTION (1.98 Å) | | Cite: | Structural basis for ligand recognition by a Cache chemosensory domain that mediates carboxylate sensing in Pseudomonas syringae.
Sci Rep, 6, 2016
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5G4Y
 | | Structural basis for carboxylic acid recognition by a Cache chemosensory domain. | | Descriptor: | Methyl-accepting chemotaxis sensory transducer with Cache sensor, UNKNOWN LIGAND | | Authors: | Brewster, J, McKellar, J.L.O, Newman, J, Peat, T.S, Gerth, M.L. | | Deposit date: | 2016-05-18 | | Release date: | 2017-03-29 | | Last modified: | 2024-01-10 | | Method: | X-RAY DIFFRACTION (2 Å) | | Cite: | Structural basis for ligand recognition by a Cache chemosensory domain that mediates carboxylate sensing in Pseudomonas syringae.
Sci Rep, 6, 2016
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7KB0
 | | O-acety-L-homoserine aminocarboxypropyltransferase (MetY) from Thermotoga maritima with pyridoxal-5-phosphate (PLP) bound in the internal aldimine state | | Descriptor: | O-acetyl-L-homoserine sulfhydrylase | | Authors: | Brewster, J.L, Pachl, P, Squire, C, Selmer, M, Patrick, W.M. | | Deposit date: | 2020-10-01 | | Release date: | 2021-06-23 | | Last modified: | 2024-04-03 | | Method: | X-RAY DIFFRACTION (1.85 Å) | | Cite: | Structures and kinetics of Thermotoga maritima MetY reveal new insights into the predominant sulfurylation enzyme of bacterial methionine biosynthesis.
J.Biol.Chem., 296, 2021
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7KB1
 | | Complex of O-acety-L-homoserine aminocarboxypropyltransferase (MetY) from Thermotoga maritima and a key reaction intermediate | | Descriptor: | (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]but-3-enoic acid, MAGNESIUM ION, O-acetyl-L-homoserine sulfhydrylase, ... | | Authors: | Brewster, J.L, Pachl, P, Squire, C, Selmer, M, Patrick, W.M. | | Deposit date: | 2020-10-01 | | Release date: | 2021-06-23 | | Last modified: | 2024-04-03 | | Method: | X-RAY DIFFRACTION (1.85 Å) | | Cite: | Structures and kinetics of Thermotoga maritima MetY reveal new insights into the predominant sulfurylation enzyme of bacterial methionine biosynthesis.
J.Biol.Chem., 296, 2021
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