1dsr
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(New page: 200px<br /><applet load="1dsr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dsr" /> '''PEPTIDE ANTIBIOTIC, NMR, 6 STRUCTURES'''<br ...)
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Revision as of 01:30, 25 November 2007
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PEPTIDE ANTIBIOTIC, NMR, 6 STRUCTURES
Overview
The 3D structure of ramoplanin was studied by NMR spectroscopy in aqueous, solution. A total of 320 interproton distances were determined from a, NOESY spectrum and were used as restraints in distance geometry, calculations. A structural refinement was carried out by molecular, dynamics calculations in a solvent box. The structure of ramoplanin is, characterized by two antiparallel beta-strands which are formed by the, residues 2-7 and 10-14, respectively. The beta-strands are connected by, six intramolecular hydrogen bonds and a reverse beta-turn which is formed, by Thr8 and Phe9 (in positions i+1 and i+2, respectively). Residues 2 and, 14 are connected by a loop consisting of Leu15, Ala16, Chp17, and the side, chain of Asn2. Although residues 14-17 show the formation of a beta-turn, only the N-terminal end of the turn is directly connected to one of the, beta-strands (Gly14), whereas the C-terminal end (Chp17) is linked via the, side chain of Asn2. The 3D conformation of ramoplanin is also stabilized, by a hydrophobic cluster of the aromatic sidechains of the residues 3, 9, and 17. This hydrophobic collapse leads to a U-shaped topology of the, beta-shee: with the beta-turn at one end and the loop at the other end., The structure found for ramoplanin differs corsiderably from the published, structure of ramoplanose which might be due to a smaller number of NOE, distance restraints used in the previous study.
About this Structure
1DSR is a Protein complex structure of sequences from Actinoplanes sp.. Full crystallographic information is available from OCA.
Reference
3D structure of ramoplanin: a potent inhibitor of bacterial cell wall synthesis., Kurz M, Guba W, Biochemistry. 1996 Sep 24;35(38):12570-5. PMID:8823194
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