1gac
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1gac" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gac" /> '''ASYMMETRIC HOMODIMER OF A82846B, A GLYCOPEPT...)
Next diff →
Revision as of 22:58, 24 November 2007
|
ASYMMETRIC HOMODIMER OF A82846B, A GLYCOPEPTIDE ANTIBIOTIC, COMPLEXED WITH ITS CELL WALL PENTAPEPTIDE FRAGMENT, NMR, 80 MODELS
Overview
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.
About this Structure
1GAC is a Protein complex structure of sequences from [1] with VAX as ligand. Full crystallographic information is available from OCA.
Reference
Conformation of A82846B, a glycopeptide antibiotic, complexed with its cell wall fragment: an asymmetric homodimer determined using NMR spectroscopy., Prowse WG, Kline AD, Skelton MA, Loncharich RJ, Biochemistry. 1995 Jul 25;34(29):9632-44. PMID:7626632
Page seeded by OCA on Sun Nov 25 01:06:11 2007
