EC Number   |
Reference  |
|---|
   7.4.2.5 | recombinant cytosolic ATP-binding domain, N-terminal His-tag |
654063 |
| 7.4.2.5 | recombinant nucleotide-binding domain |
656522 |
| 7.4.2.5 | crystals diffracting to 2.4 A resolution are obtained using the vapour-diffusion technique with sitting drops. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 203.4, b = 49.8, c = 100.8 A, alpha = gamma = 90.0°, beta = 119°. A selenomethionine derivative is prepared |
667081 |
| 7.4.2.5 | crystallization by hanging-drop vapour-diffusion technique in two different space groups P2(1(2))21 (a = b = 168.6 A, c = 149.8 A) and P6(1(5))22 (a = b = 130.9 A, c = 564.6 A). The crystals, improved by macroseeding, diffract to beyond 2.8 A and 3.5 A resolution for the trigonal and hexagonal crystal forms, respectively |
667100 |
| 7.4.2.5 | 2.8 A resolution crystal structure |
669892 |
| 7.4.2.5 | - |
699554, 700389 |
| 7.4.2.5 | homology modeling based on the crystal structure of the Shewanella oneidensis peptide transporter PepTso, identifies Glu56 and Arg305 as potential periplasmic gating residues |
719940 |
| 7.4.2.5 | EPR spectroscopy using covalently attached 2,2,5,5-tetramethylpyrrolidine-1-oxyl spin probes, and 2,2,6,6-tetramethylpiperidine-1-oxyl-4-amino-4-carboxylic acid spin-labeled peptides. The side-chains' mobility is strongly restricted at the ends of the peptide, whereas the central region is flexible, suggesting a central peptide bulge. Peptides bind to TAP in an extended kinked structure, analogous to those bound to MHC class I proteins |
720918 |
| 7.4.2.5 | molecular docking of inhibitor 2-((4-azidobenzyl)thio)-4-(4-(benzyloxy)phenyl)-6-oxo-1,6-dihydropyrimidine-5-carbonitrile. The azido group points towards hydrophilic residues including A/Asp512, A/Arg509, A/Gly510 and A/Thr511. The torsion around the -CH2O- atoms between the two phenyl groups allows the terminal phenyl group to rest in a pocket away from the hydrophilic residues B/Thr511, B/Gly510 and B/Glu487. Most of the active inhibitors seem to bind at the interface of chains A and B |
733509 |
| 7.4.2.5 | to 1.9 A resolution. Structure represents an intermediate state during the transition of the clamp from an open to a closed conformation. Closure of the clamp occurs in two phases, an initial movement of polypeptide cross-linking domain PPXD, helical scaffold domain HSD, and helical wing domain HWD as a unit, followed by a movement of PPXD alone toward nucleotide-binding domain NBD2. The substrate associates with the back of the clamp by dynamic hydrogen bonding and the clamp is laterally closed by a conserved loop of the PPXD |
734488 |
