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Title: Structure of O67745-AQUAE, a hypothetical protein from Aquifex aeolicus

Abstract

Using single-wavelength anomalous dispersion data obtained from a gold-derivatized crystal, the X-ray crystal structure of the protein 067745-AQUAE from the prokaryotic organism Aquifex aeolicus has been determined to a resolution of 2.0 Å. Using single-wavelength anomalous dispersion data obtained from a gold-derivatized crystal, the X-ray crystal structure of the protein 067745-AQUAE from the prokaryotic organism Aquifex aeolicus has been determined to a resolution of 2.0 Å. Amino-acid residues 1–371 of the 44 kDa protein were identified by Pfam as an HD domain and a member of the metal-dependent phosphohydrolase superfamily (accession No. PF01966). Although three families from this large and diverse group of enzymatic proteins are represented in the PDB, the structure of 067745-AQUAE reveals a unique fold that is unlike the others and that is likely to represent a new subfamily, further organizing the families and characterizing the proteins. Data are presented that provide the first insights into the structural organization of the proteins within this clan and a distal alternative GDP-binding domain outside the metal-binding active site is proposed.

Authors:
; ; ; ;  [1]
  1. Berkeley Structural Genomics Center, Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720 (United States)
Publication Date:
OSTI Identifier:
22360336
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal Issue: Pt 5; Other Information: PMCID: PMC2335016; PMID: 17565173; PUBLISHER-ID: sw5013; OAI: oai:pubmedcentral.nih.gov:2335016; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTAL STRUCTURE; CRYSTALS; DISPERSIONS; GOLD; PROTEINS; RESOLUTION; WAVELENGTHS

Citation Formats

Oganesyan, Vaheh, Adams, Paul D., Jancarik, Jarmila, Kim, Rosalind, and Kim, Sung-Hou, E-mail: shkim@lbl.gov. Structure of O67745-AQUAE, a hypothetical protein from Aquifex aeolicus. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107018945.
Oganesyan, Vaheh, Adams, Paul D., Jancarik, Jarmila, Kim, Rosalind, & Kim, Sung-Hou, E-mail: shkim@lbl.gov. Structure of O67745-AQUAE, a hypothetical protein from Aquifex aeolicus. United Kingdom. doi:10.1107/S1744309107018945.
Oganesyan, Vaheh, Adams, Paul D., Jancarik, Jarmila, Kim, Rosalind, and Kim, Sung-Hou, E-mail: shkim@lbl.gov. Tue . "Structure of O67745-AQUAE, a hypothetical protein from Aquifex aeolicus". United Kingdom. doi:10.1107/S1744309107018945.
@article{osti_22360336,
title = {Structure of O67745-AQUAE, a hypothetical protein from Aquifex aeolicus},
author = {Oganesyan, Vaheh and Adams, Paul D. and Jancarik, Jarmila and Kim, Rosalind and Kim, Sung-Hou, E-mail: shkim@lbl.gov},
abstractNote = {Using single-wavelength anomalous dispersion data obtained from a gold-derivatized crystal, the X-ray crystal structure of the protein 067745-AQUAE from the prokaryotic organism Aquifex aeolicus has been determined to a resolution of 2.0 Å. Using single-wavelength anomalous dispersion data obtained from a gold-derivatized crystal, the X-ray crystal structure of the protein 067745-AQUAE from the prokaryotic organism Aquifex aeolicus has been determined to a resolution of 2.0 Å. Amino-acid residues 1–371 of the 44 kDa protein were identified by Pfam as an HD domain and a member of the metal-dependent phosphohydrolase superfamily (accession No. PF01966). Although three families from this large and diverse group of enzymatic proteins are represented in the PDB, the structure of 067745-AQUAE reveals a unique fold that is unlike the others and that is likely to represent a new subfamily, further organizing the families and characterizing the proteins. Data are presented that provide the first insights into the structural organization of the proteins within this clan and a distal alternative GDP-binding domain outside the metal-binding active site is proposed.},
doi = {10.1107/S1744309107018945},
journal = {Acta Crystallographica. Section F},
number = Pt 5,
volume = 63,
place = {United Kingdom},
year = {Tue May 01 00:00:00 EDT 2007},
month = {Tue May 01 00:00:00 EDT 2007}
}