2GV1
NMR solution structure of the Acylphosphatase from Eschaerichia Coli
Summary for 2GV1
| Entry DOI | 10.2210/pdb2gv1/pdb |
| Related | 1APS 1Y9O 2ACY |
| Descriptor | Probable acylphosphatase (1 entity in total) |
| Functional Keywords | globular alpha-helix/beta-sheet protein, hydrolase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 10314.76 |
| Authors | Pagano, K.,Corazza, A.,Viglino, P.,Esposito, G. (deposition date: 2006-05-02, release date: 2006-10-31, Last modification date: 2024-10-16) |
| Primary citation | Pagano, K.,Ramazzotti, M.,Viglino, P.,Esposito, G.,Degl'innocenti, D.,Taddei, N.,Corazza, A. NMR solution structure of the acylphosphatase from Escherichia coli. J.Biomol.Nmr, 36:199-204, 2006 Cited by PubMed Abstract: The solution structure of Escherichia coli acylphosphatase (E. coli AcP), a small enzyme catalyzing the hydrolysis of acylphosphates, was determined by (1)H and (15)N NMR and restrained modelling calculation. In analogy with the other members of AcP family, E. coli AcP shows an alpha/beta sandwich domain composed of four antiparallel and one parallel beta-strand, assembled in a five-stranded beta-sheet facing two antiparallel alpha-helices. 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 2.18, 5.31 and 5.12 A, respectively. No significant differences are present in the active site region and the catalytic residue side chains are consistently positioned in the structures. PubMed: 17021943DOI: 10.1007/s10858-006-9073-2 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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