1dsr: Difference between revisions

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[[Image:1dsr.jpg|left|200px]]
{{Seed}}
[[Image:1dsr.png|left|200px]]


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{{STRUCTURE_1dsr|  PDB=1dsr  |  SCENE=  }}  
{{STRUCTURE_1dsr|  PDB=1dsr  |  SCENE=  }}  


'''PEPTIDE ANTIBIOTIC, NMR, 6 STRUCTURES'''
===PEPTIDE ANTIBIOTIC, NMR, 6 STRUCTURES===




==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}}


==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].  


==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

File:1dsr.png

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

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