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X-ray structures of two forms of the antibiotic oligomycin A: an inhibitor of ATP synthase.

Palmer RA, Ladd M, Howlin B, Lisgarten DR.

Future Med Chem. 2013 May;5(8):881-93.

School of Crystallography, Birkbeck College, University of London, Malet Street, London, WC1E 7HX, UK. [email protected]

Abstract

BACKGROUND:

Corrections to the chemical and x-ray structures of two forms of the antibiotic oligomycin A are presented: the original and best known, form (E), from Streptomyces diastatochromogenes, and a new form (C) from Streptomyces diastaticus.

METHOD:

The crystal structures are isomorphous, crystallizing in space group P212121, with Z = 4[C45H73O11.CH3OH] per unit cell. OligomycinA(E) refined with R1 = 0.0734, using Cu K{Alpha} x-radiation; and for Oligomycin A(C) R1 = 0.0651 using Mo K{Alpha} x-radiation.

CONCLUSION:

Serious corrections to the previously published structure of oligomycin A(C) are discussed and implemented. As a supplementary study geometry optimization of side group R4 of oligomycin A(E) was undertaken and achieved by energy minimization. These additional results clearly confirm the delocalization in this region observed in both x-ray structures. This result is contrary to the generally accepted formulation. Knowledge of the correct structures is important to those involved in the study and applications of the pharmacological and biological properties of these materials.

 

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Additional Information:

 

The authors affiliations and interests:

Rex A. Palmer:

School of Crystallography, Birkbeck College, University of London, UK

Structure and function of biologically active molecules

Mark Ladd:

Formerly of  Chemical Physics, University of Surrey, Guildford, UK

X-ray crystallography, chemical bonding, structure analysis

Brendan Howlin:

Chemical Sciences Division, Faculty of Health and Medical Sciences, University of Surrey, Guildford, UK

Structure, molecular modeling and molecular dynamics of biological structures

David R Lisgarten:

Department of Geographical and Life Sciences, Canterbury Christ Church University, UK
X-ray crystallography of biologically active molecules, molecular modelling and molecular dynamics.

 

X ray structures of two forms of the antibiotic oligomycin A an inhibitor of ATP synthase.

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

The authors affiliations and interests:

Rex A. Palmer:

School of Crystallography, Birkbeck College, University of London, UK

Structure and function of biologically active molecules.

 

Mark Ladd:

Formerly of  Chemical Physics, University of Surrey, Guildford, UK

X-ray crystallography, chemical bonding, structure analysis.

 

Brendan Howlin:

Chemical Sciences Division, Faculty of Health and Medical Sciences, University of Surrey, Guildford, UK

Structure, molecular modeling and molecular dynamics of biological structures.

 

David R Lisgarten:

Department of Geographical and Life Sciences, Canterbury Christ Church University, UK
X-ray crystallography of biologically active molecules, molecular modelling and molecular dynamics