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Title: The structure at 2.4 Å resolution of the protein from gene locus At3g21360, a putative Fe{sup II}/2-oxoglutarate-dependent enzyme from Arabidopsis thaliana

Abstract

The crystal structure of the 37.2 kDa At3g21360 gene product from A. thaliana was determined at 2.4 Å resolution. The structure establishes that this protein binds a metal ion and is a member of a clavaminate synthase-like superfamily in A. thaliana. The crystal structure of the gene product of At3g21360 from Arabidopsis thaliana was determined by the single-wavelength anomalous dispersion method and refined to an R factor of 19.3% (R{sub free} = 24.1%) at 2.4 Å resolution. The crystal structure includes two monomers in the asymmetric unit that differ in the conformation of a flexible domain that spans residues 178–230. The crystal structure confirmed that At3g21360 encodes a protein belonging to the clavaminate synthase-like superfamily of iron(II) and 2-oxoglutarate-dependent enzymes. The metal-binding site was defined and is similar to the iron(II) binding sites found in other members of the superfamily.

Authors:
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  1. Center for Eukaryotic Structural Genomics, Department of Biochemistry, University of Wisconsin-Madison (United States)
Publication Date:
OSTI Identifier:
22355991
Resource Type:
Journal Article
Journal Name:
Acta Crystallographica. Section F
Additional Journal Information:
Journal Volume: 61; Journal Issue: Pt 5; Other Information: PMCID: PMC1952295; PMID: 16511070; PUBLISHER-ID: gx5053; OAI: oai:pubmedcentral.nih.gov:1952295; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTAL STRUCTURE; DISPERSIONS; IONS; IRON; MONOMERS; R FACTORS; RESOLUTION; WAVELENGTHS

Citation Formats

Bitto, Eduard, Bingman, Craig A., Allard, Simon T. M., Wesenberg, Gary E., Aceti, David J., Wrobel, Russell L., Frederick, Ronnie O., Sreenath, Hassan, Vojtik, Frank C., Jeon, Won Bae, Newman, Craig S., Primm, John, Sussman, Michael R., Fox, Brian G., Markley, John L., and Phillips, Jr, George N. The structure at 2.4 Å resolution of the protein from gene locus At3g21360, a putative Fe{sup II}/2-oxoglutarate-dependent enzyme from Arabidopsis thaliana. United Kingdom: N. p., 2005. Web. doi:10.1107/S1744309105011565.
Bitto, Eduard, Bingman, Craig A., Allard, Simon T. M., Wesenberg, Gary E., Aceti, David J., Wrobel, Russell L., Frederick, Ronnie O., Sreenath, Hassan, Vojtik, Frank C., Jeon, Won Bae, Newman, Craig S., Primm, John, Sussman, Michael R., Fox, Brian G., Markley, John L., & Phillips, Jr, George N. The structure at 2.4 Å resolution of the protein from gene locus At3g21360, a putative Fe{sup II}/2-oxoglutarate-dependent enzyme from Arabidopsis thaliana. United Kingdom. https://doi.org/10.1107/S1744309105011565
Bitto, Eduard, Bingman, Craig A., Allard, Simon T. M., Wesenberg, Gary E., Aceti, David J., Wrobel, Russell L., Frederick, Ronnie O., Sreenath, Hassan, Vojtik, Frank C., Jeon, Won Bae, Newman, Craig S., Primm, John, Sussman, Michael R., Fox, Brian G., Markley, John L., and Phillips, Jr, George N. 2005. "The structure at 2.4 Å resolution of the protein from gene locus At3g21360, a putative Fe{sup II}/2-oxoglutarate-dependent enzyme from Arabidopsis thaliana". United Kingdom. https://doi.org/10.1107/S1744309105011565.
@article{osti_22355991,
title = {The structure at 2.4 Å resolution of the protein from gene locus At3g21360, a putative Fe{sup II}/2-oxoglutarate-dependent enzyme from Arabidopsis thaliana},
author = {Bitto, Eduard and Bingman, Craig A. and Allard, Simon T. M. and Wesenberg, Gary E. and Aceti, David J. and Wrobel, Russell L. and Frederick, Ronnie O. and Sreenath, Hassan and Vojtik, Frank C. and Jeon, Won Bae and Newman, Craig S. and Primm, John and Sussman, Michael R. and Fox, Brian G. and Markley, John L. and Phillips, Jr, George N.},
abstractNote = {The crystal structure of the 37.2 kDa At3g21360 gene product from A. thaliana was determined at 2.4 Å resolution. The structure establishes that this protein binds a metal ion and is a member of a clavaminate synthase-like superfamily in A. thaliana. The crystal structure of the gene product of At3g21360 from Arabidopsis thaliana was determined by the single-wavelength anomalous dispersion method and refined to an R factor of 19.3% (R{sub free} = 24.1%) at 2.4 Å resolution. The crystal structure includes two monomers in the asymmetric unit that differ in the conformation of a flexible domain that spans residues 178–230. The crystal structure confirmed that At3g21360 encodes a protein belonging to the clavaminate synthase-like superfamily of iron(II) and 2-oxoglutarate-dependent enzymes. The metal-binding site was defined and is similar to the iron(II) binding sites found in other members of the superfamily.},
doi = {10.1107/S1744309105011565},
url = {https://www.osti.gov/biblio/22355991}, journal = {Acta Crystallographica. Section F},
issn = {1744-3091},
number = Pt 5,
volume = 61,
place = {United Kingdom},
year = {Sun May 01 00:00:00 EDT 2005},
month = {Sun May 01 00:00:00 EDT 2005}
}