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Structure of O67745_AQUAE, a hypothetical protein from Aquifex aeolicus
Author(s) -
Oganesyan Vaheh,
Kim Rosalind,
Adams Paul D.,
Jancarik Jarmila,
Kim SungHou
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107018945
Subject(s) - aquifex aeolicus , protein data bank (rcsb pdb) , subfamily , structural genomics , crystallography , hydrolase , protein data bank , domain (mathematical analysis) , protein structure , chemistry , biology , computational biology , enzyme , biochemistry , gene , mathematics , mathematical analysis , escherichia coli
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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