NMR solution structure of type-B lantibiotics mersacidin bound to lipid II in
DPC micelles

Two distinct conformations were obtained for the glycine-rich ring (residues
5-11) and models 1-9 and models 10-17 belong to those clusters, respectively.

Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
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Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Mon Jul 25 12:49:16 2011

NMR study of mersacidin and lipid II interaction in dodecylphosphocholine micelles. Conformational changes are a key to antimicrobial activity.

The crystal structure of mersacidin, a potential novel antibiotic against
methicillin- and vancomycin-resistant Staphylococcus aureus strains, has been
determined by ab initio methods. Despite all crystals being merohedrally
twinned, an accurate structural model with an R value of 13.4% has been
obtained at atomic resolution. With six molecules in the asymmetric unit and no
atom heavier than sulfur, the structure corresponds to a protein of 120 amino
acids and is the largest approximately equal-atom unknown structure solved by
direct methods. In the crystal, the molecule assumes a compact fold different
from that found by NMR in solution. Comparison of the NCS-related molecules
reveals regions of variable flexibility. The region highly homologous to the
related antibiotic actagardine is very rigid and possibly defines an essential
building block of this class of new antibacterial substances.

Schneider TR, Karcher J, Pohl E, Lubini P, Sheldrick GM.
Ab initio structure determination of the lantibiotic mersacidin.
Acta Crystallogr D Biol Crystallogr. 2000 Jun;56 (Pt 6):705-13.

Acta crystallographica. Section D, Biological crystallography
Ab initio structure determination of the lantibiotic mersacidin.

The solution structure of the tetracyclic lantibiotic mersacidin in methanol
(CD3OH) has been determined by NMR followed by distance bound driven dynamics
and subsequent restrained molecular dynamics simulations combined with an
iterative relaxation matrix approach and alternatively by a simulated annealing
protocol. The molecular dynamics simulations were performed with the AMBER
program system and with the INSIGHT program package. The distance bound driven
dynamics calculation was conducted using a modified version of the DISGEO II
program. The interproton distance restraints were derived from jump symmetrized
rotating-frame Overhauser enhancement and exchange (JS-ROESY) spectra, which
yield optimum sensitivity for medium-sized molecules like mersacidin. The
connectivities via the sulfide bridges were unambiguously confirmed by
heteronuclear NMR techniques (heteronuclear single quantum coherence and
heteronuclear multiple bond correlation methods). Due to the tetracyclic
structure, mersacidin exhibits a rather rigid globular shape, which neither
belongs to the duramycin nor to the nisin structure type lantibiotics. The
resulting structures for the simulated annealing protocol of restrained and
subsequent free molecular dynamics were compared and found to be very similar.

Prasch T, Naumann T, Markert RL, Sattler M, Schubert W, Schaal S, Bauch M, Kogler
H, Griesinger C.
Constitution and solution conformation of the antibiotic mersacidin determined by NMR and molecular
dynamics.
Eur J Biochem. 1997 Mar 1;244(2):501-12.

Constitution and solution conformation of the antibiotic mersacidin determined by NMR and molecular dynamics.

A Chain A, Nmr Solution Structure Of Type-BLantibiotics Mersacidin In MeohH2O MIXTURE

A Chain A, Nmr Solution Structure Of Type-BLantibiotics Mersacidin In Dpc Micelles

A Chain A, Nmr Solution Structure Of Type-BLantibiotics Mersacidin Bound To Lipid Ii In DpcMicelles

SIMULATED ANNEALING TORSION, ANGLE DYNAMICS

free form lantibiotics mersacidin in MeOH/H2O.

free form lantibiotics mersacidin in DPC micelles.