NDLI: Racemic crystallography of synthetic protein enantiomers used to determine the X-ray structure of plectasin by direct methods

Content Provider	PubMed Central
Author	Mandal, Kalyaneswar Pentelute, Brad L. Valentina, Tereshko Thammavongsa, Vilasak Schneewind, Olaf Kossiakoff, Anthony A. Kent, Stephen B. H.
Abstract	We describe the use of racemic crystallography to determine the X-ray structure of the natural product plectasin, a potent antimicrobial protein recently isolated from fungus. The protein enantiomers l-plectasin and d-plectasin were prepared by total chemical synthesis; interestingly, l-plectasin showed the expected antimicrobial activity, while d-plectasin was devoid of such activity. The mirror image proteins were then used for racemic crystallization. Synchrotron X-ray diffraction data were collected to atomic resolution from a racemic plectasin crystal; the racemate crystallized in the achiral centrosymmetric space group with one l-plectasin molecule and one d-plectasin molecule forming the unit cell. Dimer-like intermolecular interactions between the protein enantiomers were observed, which may account for the observed extremely low solvent content (13%–15%) and more highly ordered nature of the racemic crystals. The structure of the plectasin molecule was well defined for all 40 amino acids and was generally similar to the previously determined NMR structure, suggesting minimal impact of the crystal packing on the plectasin conformation.
Related Links	http://dx.doi.org/10.1002/pro.127
Ending Page	1154
Page Count	9
Starting Page	1146
File Format	PDF
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science : A Publication of the Protein Society
Issue Number	6
Volume Number	18
Language	English
Publisher	Wiley Subscription Services, Inc., A Wiley Company
Publisher Date	2009-06-01
Access Restriction	Open
Rights Holder	Wiley Subscription Services, Inc., A Wiley Company
Subject Keyword	Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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