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

Here, 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. In conclusion, 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. Proteins 2015; 83:383–388.
Authors:
 [1] ;  [2] ;  [3] ;  [4] ;  [5] ;  [2] ;  [4] ;  [2] ;  [2] ;  [1] ;  [4]
  1. Univ. of Wisconsin-Madison, Madison, WI (United States). Dept. of Bacteriology
  2. Argonne National Lab. (ANL), Argonne, IL (United States). Biosciences Division
  3. Univ. of Wisconsin-Madison, Madison, WI (United States). Dept. of Biochemistry
  4. Rice Univ., Houston TX (United States). Biosciences
  5. Structural Biology Center, Biosciences Division, Argonne National Laboratory, Argonne Illinois
Publication Date:
OSTI Identifier:
1263631
Grant/Contract Number:
AC02-06CH11357; GM098248; GM094585
Type:
Accepted Manuscript
Journal Name:
Proteins
Additional Journal Information:
Journal Volume: 83; Journal Issue: 2; Journal ID: ISSN 0887-3585
Publisher:
Wiley
Research Org:
Argonne National Laboratory (ANL), Argonne, IL (United States)
Sponsoring Org:
USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES cupin; X-ray; structural genomics; natural product; manganese-bound