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Title of Journal: J Biomol NMR

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Abbravation: Journal of Biomolecular NMR

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Kluwer Academic Publishers

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DOI

10.1007/0-387-21749-5_4

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1573-5001

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NMR solution structure of the acylphosphatase from

Authors: Katiuscia Pagano Matteo Ramazzotti Paolo Viglino Gennaro Esposito Donatella Degl’Innocenti Niccolò Taddei Alessandra Corazza
Publish Date: 2006/10/05
Volume: 36, Issue: 3, Pages: 199-204
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Abstract

The solution structure of Escherichia coli acylphosphatase E coli AcP a small enzyme catalyzing the hydrolysis of acylphosphates was determined by 1H and 15N NMR and restrained modelling calculation In analogy with the other members of AcP family E coli AcP shows an α/β sandwich domain composed of four antiparallel and one parallel βstrand assembled in a fivestranded βsheet facing two antiparallel αhelices The pairwise RMSD values calculated for the backbone atoms of E coli and Sulfolobus solfataricus AcP Bovine common type AcP and Horse muscle AcP are 218 531 and 512 Å respectively No significant differences are present in the active site region and the catalytic residue side chains are consistently positioned in the structures

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  2. Statistical removal of background signals from high-throughput 1 H NMR line-broadening ligand-affinity screens
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  7. Selective 1 H- 13 C NMR spectroscopy of methyl groups in residually protonated samples of large proteins
  8. Fast methionine-based solution structure determination of calcium-calmodulin complexes
  9. A procedure to validate and correct the 13 C chemical shift calibration of RNA datasets
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  12. S3EPY: a Sparky extension for determination of small scalar couplings from spin-state-selective excitation NMR experiments
  13. Improved NMR experiments with 13 C-isotropic mixing for assignment of aromatic and aliphatic side chains in labeled proteins
  14. Out-and-back 13 C– 13 C scalar transfers in protein resonance assignment by proton-detected solid-state NMR under ultra-fast MAS
  15. Perspectives for sensitivity enhancement in proton-detected solid-state NMR of highly deuterated proteins by preserving water magnetization
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  17. Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids
  18. Use of quantitative 1 H NMR chemical shift changes for ligand docking into barnase
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