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Title: The structure at 1.7 Å resolution of the protein product of the At2g17340 gene from Arabidopsis thaliana

Abstract

The crystal structure of the 40.8 kDa At2g17340 protein from A. thaliana was determined at 1.7 Å resolution. The structure provides the first insight into the structural organization of the Pfam01937.11 family and establishes that the proteins of this family coordinate a metal in its putative active site. The crystal structure of the At2g17340 protein from A. thaliana was determined by the multiple-wavelength anomalous diffraction method and was refined to an R factor of 16.9% (R{sub free} = 22.1%) at 1.7 Å resolution. At2g17340 is a member of the Pfam01937.11 protein family and its structure provides the first insight into the structural organization of this family. A number of fully and highly conserved residues defined by multiple sequence alignment of members of the Pfam01937.11 family were mapped onto the structure of At2g17340. The fully conserved residues are involved in the coordination of a metal ion and in the stabilization of loops surrounding the metal site. Several additional highly conserved residues also map into the vicinity of the metal-binding site, while others are clearly involved in stabilizing the hydrophobic core of the protein. The structure of At2g17340 represents a new fold in protein conformational space.

Authors:
; ; ; ;  [1]
  1. Center for Eukaryotic Structural Genomics, Department of Biochemistry, University of Wisconsin-Madison (United States)
Publication Date:
OSTI Identifier:
22356143
Resource Type:
Journal Article
Journal Name:
Acta Crystallographica. Section F
Additional Journal Information:
Journal Volume: 61; Journal Issue: Pt 7; Other Information: PMCID: PMC1952457; PMID: 16511115; PUBLISHER-ID: gx5063; OAI: oai:pubmedcentral.nih.gov:1952457; 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; ALIGNMENT; CRYSTAL STRUCTURE; IONS; METALS; PROTEINS; R FACTORS; RESOLUTION; STABILIZATION; WAVELENGTHS

Citation Formats

Bitto, Eduard, Bingman, Craig A., Allard, Simon T. M., Wesenberg, Gary E., and Phillips, Jr, George N. The structure at 1.7 Å resolution of the protein product of the At2g17340 gene from Arabidopsis thaliana. United Kingdom: N. p., 2005. Web. doi:10.1107/S1744309105017690.
Bitto, Eduard, Bingman, Craig A., Allard, Simon T. M., Wesenberg, Gary E., & Phillips, Jr, George N. The structure at 1.7 Å resolution of the protein product of the At2g17340 gene from Arabidopsis thaliana. United Kingdom. https://doi.org/10.1107/S1744309105017690
Bitto, Eduard, Bingman, Craig A., Allard, Simon T. M., Wesenberg, Gary E., and Phillips, Jr, George N. 2005. "The structure at 1.7 Å resolution of the protein product of the At2g17340 gene from Arabidopsis thaliana". United Kingdom. https://doi.org/10.1107/S1744309105017690.
@article{osti_22356143,
title = {The structure at 1.7 Å resolution of the protein product of the At2g17340 gene from Arabidopsis thaliana},
author = {Bitto, Eduard and Bingman, Craig A. and Allard, Simon T. M. and Wesenberg, Gary E. and Phillips, Jr, George N.},
abstractNote = {The crystal structure of the 40.8 kDa At2g17340 protein from A. thaliana was determined at 1.7 Å resolution. The structure provides the first insight into the structural organization of the Pfam01937.11 family and establishes that the proteins of this family coordinate a metal in its putative active site. The crystal structure of the At2g17340 protein from A. thaliana was determined by the multiple-wavelength anomalous diffraction method and was refined to an R factor of 16.9% (R{sub free} = 22.1%) at 1.7 Å resolution. At2g17340 is a member of the Pfam01937.11 protein family and its structure provides the first insight into the structural organization of this family. A number of fully and highly conserved residues defined by multiple sequence alignment of members of the Pfam01937.11 family were mapped onto the structure of At2g17340. The fully conserved residues are involved in the coordination of a metal ion and in the stabilization of loops surrounding the metal site. Several additional highly conserved residues also map into the vicinity of the metal-binding site, while others are clearly involved in stabilizing the hydrophobic core of the protein. The structure of At2g17340 represents a new fold in protein conformational space.},
doi = {10.1107/S1744309105017690},
url = {https://www.osti.gov/biblio/22356143}, journal = {Acta Crystallographica. Section F},
issn = {1744-3091},
number = Pt 7,
volume = 61,
place = {United Kingdom},
year = {Fri Jul 01 00:00:00 EDT 2005},
month = {Fri Jul 01 00:00:00 EDT 2005}
}