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| {{STRUCTURE_1dsr| PDB=1dsr | SCENE= }} | | {{STRUCTURE_1dsr| PDB=1dsr | SCENE= }} |
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- | '''PEPTIDE ANTIBIOTIC, NMR, 6 STRUCTURES'''
| + | ===PEPTIDE ANTIBIOTIC, NMR, 6 STRUCTURES=== |
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- | ==Overview==
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- | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8823194}}, adds the Publication Abstract to the page |
| + | (as it appears on PubMed at http://www.pubmed.gov), where 8823194 is the PubMed ID number. |
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| + | {{ABSTRACT_PUBMED_8823194}} |
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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]. | + | Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DSR OCA]. |
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| ==Reference== | | ==Reference== |
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| [[Category: Inhibitor]] | | [[Category: Inhibitor]] |
| [[Category: Ramoplanin]] | | [[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 Mon Jun 30 23:33:36 2008'' |
Revision as of 20:33, 30 June 2008
Template:STRUCTURE 1dsr
PEPTIDE ANTIBIOTIC, NMR, 6 STRUCTURES
Template:ABSTRACT PUBMED 8823194
About this Structure
Full experimental 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 Mon Jun 30 23:33:36 2008