1dsr
From Proteopedia
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'''PEPTIDE ANTIBIOTIC, NMR, 6 STRUCTURES''' | '''PEPTIDE ANTIBIOTIC, NMR, 6 STRUCTURES''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DSR OCA]. | |
==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/8823194 8823194] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8823194 8823194] | ||
| - | [[Category: Actinoplanes sp.]] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Guba, W.]] | [[Category: Guba, W.]] | ||
[[Category: Kurz, M.]] | [[Category: Kurz, M.]] | ||
| - | [[Category: | + | [[Category: Antibiotic]] |
| - | [[Category: | + | [[Category: Inhibitor]] |
| - | [[Category: | + | [[Category: Ramoplanin]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:13:46 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 11:13, 2 May 2008
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
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 Page seeded by OCA on Fri May 2 14:13:46 2008
Categories: Guba, W. | Kurz, M. | Antibiotic | Inhibitor | Ramoplanin
