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Title: Structure of a cupin protein Plu4264 from Photorhabdus luminescens subsp. laumondii TTO1 at 1.35 Å resolution: Cupin Structure from Photorhabdus luminescens

Abstract

Proteins belonging to the cupin superfamily have a wide range of catalytic and noncatalytic functions. Cupin proteins commonly have the capacity to bind a metal ion with the metal frequently determining the function of the protein. We have been investigating the function of homologous cupin proteins that are conserved in more than 40 species of bacteria. To gain insights into the potential function of these proteins we have solved the structure of Plu4264 from Photorhabdus luminescens TTO1 at a resolution of 1.35 Å and identified manganese as the likely natural metal ligand of the protein.

Authors:
 [1];  [2];  [3];  [4];  [5];  [5];  [4];  [2];  [2];  [1];  [4]
  1. Department of Bacteriology, University of Wisconsin-Madison, Madison Wisconsin
  2. Midwest Center for Structural Genomics, Biosciences Division, Argonne National Laboratory, Argonne Illinois; Structural Biology Center, Biosciences Division, Argonne National Laboratory, Argonne Illinois
  3. Department of Biochemistry, University of Wisconsin-Madison, Madison Wisconsin
  4. Biosciences at Rice, Rice University, Houston Texas
  5. Structural Biology Center, Biosciences Division, Argonne National Laboratory, Argonne Illinois
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23)
OSTI Identifier:
1391830
DOE Contract Number:  
AC02-06CH11357
Resource Type:
Journal Article
Journal Name:
Proteins
Additional Journal Information:
Journal Volume: 83; Journal Issue: 2; Journal ID: ISSN 0887-3585
Publisher:
Wiley
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES

Citation Formats

Weerth, R. Sophia, Michalska, Karolina, Bingman, Craig A., Yennamalli, Ragothaman M., Li, Hui, Jedrzejczak, Robert, Wang, Fengbin, Babnigg, Gyorgy, Joachimiak, Andrzej, Thomas, Michael G., and Phillips, George N. Structure of a cupin protein Plu4264 from Photorhabdus luminescens subsp. laumondii TTO1 at 1.35 Å resolution: Cupin Structure from Photorhabdus luminescens. United States: N. p., 2014. Web. doi:10.1002/prot.24705.
Weerth, R. Sophia, Michalska, Karolina, Bingman, Craig A., Yennamalli, Ragothaman M., Li, Hui, Jedrzejczak, Robert, Wang, Fengbin, Babnigg, Gyorgy, Joachimiak, Andrzej, Thomas, Michael G., & Phillips, George N. Structure of a cupin protein Plu4264 from Photorhabdus luminescens subsp. laumondii TTO1 at 1.35 Å resolution: Cupin Structure from Photorhabdus luminescens. United States. doi:10.1002/prot.24705.
Weerth, R. Sophia, Michalska, Karolina, Bingman, Craig A., Yennamalli, Ragothaman M., Li, Hui, Jedrzejczak, Robert, Wang, Fengbin, Babnigg, Gyorgy, Joachimiak, Andrzej, Thomas, Michael G., and Phillips, George N. Thu . "Structure of a cupin protein Plu4264 from Photorhabdus luminescens subsp. laumondii TTO1 at 1.35 Å resolution: Cupin Structure from Photorhabdus luminescens". United States. doi:10.1002/prot.24705.
@article{osti_1391830,
title = {Structure of a cupin protein Plu4264 from Photorhabdus luminescens subsp. laumondii TTO1 at 1.35 Å resolution: Cupin Structure from Photorhabdus luminescens},
author = {Weerth, R. Sophia and Michalska, Karolina and Bingman, Craig A. and Yennamalli, Ragothaman M. and Li, Hui and Jedrzejczak, Robert and Wang, Fengbin and Babnigg, Gyorgy and Joachimiak, Andrzej and Thomas, Michael G. and Phillips, George N.},
abstractNote = {Proteins belonging to the cupin superfamily have a wide range of catalytic and noncatalytic functions. Cupin proteins commonly have the capacity to bind a metal ion with the metal frequently determining the function of the protein. We have been investigating the function of homologous cupin proteins that are conserved in more than 40 species of bacteria. To gain insights into the potential function of these proteins we have solved the structure of Plu4264 from Photorhabdus luminescens TTO1 at a resolution of 1.35 Å and identified manganese as the likely natural metal ligand of the protein.},
doi = {10.1002/prot.24705},
journal = {Proteins},
issn = {0887-3585},
number = 2,
volume = 83,
place = {United States},
year = {2014},
month = {12}
}

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