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Acta Crystallogr Sect F Struct Biol Cryst Commun. May 1, 2007; 63(Pt 5): 369–374.
Published online Apr 28, 2007. doi:  10.1107/S1744309107018945
PMCID: PMC2335016
Structure of O67745_AQUAE, a hypothetical protein from Aquifex aeolicus
Vaheh Oganesyan,a Paul D. Adams,a Jarmila Jancarik,a Rosalind Kim,a and Sung-Hou Kima*
aBerkeley Structural Genomics Center, Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA
Correspondence e-mail: shkim/at/lbl.gov
Received August 18, 2006; Accepted April 16, 2007.
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. 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.
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International Union of Crystallography