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

Journal Article · · Proteins
DOI:https://doi.org/10.1002/prot.24705· OSTI ID:1263631
 [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
+ Show Author Affiliations

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. Proteins 2015; 83:383–388. © 2014 Wiley Periodicals, Inc.

Research Organization:
Argonne National Laboratory (ANL), Argonne, IL (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Biological and Environmental Research (BER)
Grant/Contract Number:
AC02-06CH11357; GM098248; GM094585
OSTI ID:
1263631
Alternate ID(s):
OSTI ID: 1400881
Journal Information:
Proteins, Vol. 83, Issue 2; ISSN 0887-3585
Publisher:
WileyCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 3 works
Citation information provided by
Web of Science

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Cited By (3)

Integrating Experiment and Theory to Understand TCR-pMHC Dynamics journal December 2018
Loop dynamics of thymidine diphosphate-rhamnose 3′-O-methyltransferase (CalS11), an enzyme in calicheamicin biosynthesis journal January 2016
Identifying and Visualizing Macromolecular Flexibility in Structural Biology journal September 2016

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Related Subjects

59 BASIC BIOLOGICAL SCIENCES
cupin
X-ray
structural genomics
natural product
manganese-bound