X‐Ray structure of the antibiotic bacitracin A

FEBS Letters

Branner, Sven³  Pfeffer, Sabine¹  Betzel, Christian¹  Höhne, Wolfgang²  Wilson, Keith¹ 

[1] European Molecular Biology Laboratory, c/o DESY, Notkestraße 85, 2000 Hamburg 52, Germany;Institut für Biochemie, Humboldt-Universität Berlin Hessische Straße 3-4, 104O Berlin, Germany;NOVO-NORDISK, Novo Alle, DK-288O Bagsvaerd, Denmark

关键词: Antibiotic peptide;    X-ray structure;    Synchrotron radiation;   

DOI  :  10.1016/0014-5793(91)80738-O

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Bacitracins are a group of widely used peptide antibiotics. There has been interest in determining the three-dimensional structure of the bacitracins. However, solution studies indicate significant flexibility in their structure and to date native bacitracins have resisted attempts at crystallisation despite considerable efforts over a number of years by several groups. Here we report the first three-dimensional X-ray structure of a bacitracin, complexed to a subtilisin proteinase. X-Ray diffraction data were collected using synchrotron radiation in combination with the Image Plate Scanner system. The complex structure including two enzymes, two bacitracins, 220 water molecules and two Ca²⁺ ions was refined by restrained least-squares to a crystallographic R factor (=Σ{{F _o-F _c}}/Σ{F _o}}) of 16.3% at 2.0 Å.

【 授权许可】

Unknown