1GAC
NMR structure of asymmetric homodimer of a82846b, a glycopeptide antibiotic, complexed with its cell wall pentapeptide fragment
Summary for 1GAC
| Entry DOI | 10.2210/pdb1gac/pdb |
| Related | 1AA5 1C0Q 1C0R 1FVM 1GHG 1PN3 1PNV 1QD8 1RRV 1SHO |
| Related PRD ID | PRD_000203 |
| Descriptor | CELL WALL PENTAPEPTIDE, CHLOROORIENTICIN A, vancosamine-(1-2)-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | peptide-antibiotic complex, cell wall peptide, glycopeptide, antibiotic, vancomycin peptide-antibiotic complex, peptide/antibiotic |
| Biological source | AMYCOLATOPSIS ORIENTALIS More |
| Total number of polymer chains | 4 |
| Total formula weight | 4248.12 |
| Authors | Kline, A.D.,Prowse, W.G.,Skelton, M.A.,Loncharich, R.J. (deposition date: 1995-05-24, release date: 1996-08-17, Last modification date: 2023-11-15) |
| Primary citation | Prowse, W.G.,Kline, A.D.,Skelton, M.A.,Loncharich, R.J. Conformation of A82846B, a Glycopeptide Antibiotic, Complexed with its Cell Wall Fragment: An Asymmetric Homodimer Determined Using NMR Spectroscopy. Biochemistry, 34:9632-, 1995 Cited by PubMed Abstract: Proton NMR assignments were determined for the asymmetric dimer complex of A82846B with the pentapeptide cell-wall fragment. A total of 683 experimental constraints, both distance and dihedral, were collected from NOESY and COSY data sets. From these constraints, a total of 80 structures were calculated using standard X-PLOR protocols. These structures were subsequently refined using the full CHARMm potential and the addition of water molecules in the calculation. The CHARMm structures occupied more conformational space than did the X-PLOR structures and were utilized for the structure analysis. From the structures, a unique set of interactions for the dALA-5 carboxylate pocket was observed, having backbone amides from residues 2 and 3 hydrogen bonding one carboxylate oxygen while amide 4 and the side chain amide from Asn-3 hydrogen bond the other oxygen. Also, near the N-terminal region of the ligand, the GGLU-2's carboxylate forms a hydrogen bond with the asymmetric disaccharide dyad, which helps to define the interactions seen for this part of the ligand. PubMed: 7626632DOI: 10.1021/BI00029A041 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
