1dsr
From Proteopedia
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| - | [[Image:1dsr.jpg|left|200px]] | + | [[Image:1dsr.jpg|left|200px]] |
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| - | '''PEPTIDE ANTIBIOTIC, NMR, 6 STRUCTURES''' | + | {{Structure |
| + | |PDB= 1dsr |SIZE=350|CAPTION= <scene name='initialview01'>1dsr</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''PEPTIDE ANTIBIOTIC, NMR, 6 STRUCTURES''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DSR is a [ | + | 1DSR is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Actinoplanes_sp. Actinoplanes sp.]. 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:// | + | 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: Actinoplanes sp.]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: ramoplanin]] | [[Category: ramoplanin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:43:44 2008'' |
Revision as of 08:43, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
Page seeded by OCA on Thu Mar 20 10:43:44 2008
