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Title: Retention of Native Quaternary Structure in Racemic Melittin Crystals

Abstract

Racemic crystallography has been used to elucidate the secondary and tertiary structures of peptides and small proteins that are recalcitrant to conventional crystallization. It is unclear, however, whether racemic crystallography can capture native quaternary structure, which could be disrupted by heterochiral associations. We are exploring the use of racemic crystallography to characterize the self-assembly behavior of membrane-associated peptides, very few of which have been crystallized. We report a racemic crystal structure of the membrane-active peptide melittin; the new structure allows comparison with a previously reported crystal structure of L-melittin. The tetrameric assembly observed in crystalline L-melittin has been proposed to represent the tetrameric state detected in solution for this peptide. This tetrameric assembly is precisely reproduced in the racemic crystal, which strengthens the conclusion that the tetramer is biologically relevant. More broadly, these findings suggest that racemic crystallography can provide insight on native quaternary structure.

Authors:
ORCiD logo [1];  [1];  [1]; ORCiD logo [2];  [1];  [1]; ORCiD logo [1]
  1. Univ. of Wisconsin, Madison, WI (United States)
  2. Univ. at Buffalo, NY (United States)
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
NSFNIH
OSTI Identifier:
1526066
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Journal of the American Chemical Society
Additional Journal Information:
Journal Volume: 141; Journal Issue: 19; Journal ID: ISSN 0002-7863
Publisher:
American Chemical Society (ACS)
Country of Publication:
United States
Language:
ENGLISH
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; Crystals; Peptides and proteins; Crystal structure; Oligomers; Molecules

Citation Formats

Kurgan, Kathleen W., Kleman, Adam F., Bingman, Craig A., Kreitler, Dale F., Weisblum, Bernard, Forest, Katrina T., and Gellman, Samuel H. Retention of Native Quaternary Structure in Racemic Melittin Crystals. United States: N. p., 2019. Web. doi:10.1021/jacs.9b02691.
Kurgan, Kathleen W., Kleman, Adam F., Bingman, Craig A., Kreitler, Dale F., Weisblum, Bernard, Forest, Katrina T., & Gellman, Samuel H. Retention of Native Quaternary Structure in Racemic Melittin Crystals. United States. https://doi.org/10.1021/jacs.9b02691
Kurgan, Kathleen W., Kleman, Adam F., Bingman, Craig A., Kreitler, Dale F., Weisblum, Bernard, Forest, Katrina T., and Gellman, Samuel H. Mon . "Retention of Native Quaternary Structure in Racemic Melittin Crystals". United States. https://doi.org/10.1021/jacs.9b02691. https://www.osti.gov/servlets/purl/1526066.
@article{osti_1526066,
title = {Retention of Native Quaternary Structure in Racemic Melittin Crystals},
author = {Kurgan, Kathleen W. and Kleman, Adam F. and Bingman, Craig A. and Kreitler, Dale F. and Weisblum, Bernard and Forest, Katrina T. and Gellman, Samuel H.},
abstractNote = {Racemic crystallography has been used to elucidate the secondary and tertiary structures of peptides and small proteins that are recalcitrant to conventional crystallization. It is unclear, however, whether racemic crystallography can capture native quaternary structure, which could be disrupted by heterochiral associations. We are exploring the use of racemic crystallography to characterize the self-assembly behavior of membrane-associated peptides, very few of which have been crystallized. We report a racemic crystal structure of the membrane-active peptide melittin; the new structure allows comparison with a previously reported crystal structure of L-melittin. The tetrameric assembly observed in crystalline L-melittin has been proposed to represent the tetrameric state detected in solution for this peptide. This tetrameric assembly is precisely reproduced in the racemic crystal, which strengthens the conclusion that the tetramer is biologically relevant. More broadly, these findings suggest that racemic crystallography can provide insight on native quaternary structure.},
doi = {10.1021/jacs.9b02691},
url = {https://www.osti.gov/biblio/1526066}, journal = {Journal of the American Chemical Society},
issn = {0002-7863},
number = 19,
volume = 141,
place = {United States},
year = {2019},
month = {5}
}

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Cited by: 3 works
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