Open AccessStructure of putative CutA1 from Homo sapiens determined at 2.05 Å resolution
Author(s) -
Bagautdinov Bagautdin,
Matsuura Yoshinori,
Bagautdinova Svetlana,
Kunishima Naoki,
Yutani Katsuhide
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108009846
Subject(s) - antiparallel (mathematics) , crystallography , crystal structure , trimer , molecule , structural similarity , resolution (logic) , chemistry , protein subunit , protein structure , stereochemistry , biophysics , biology , biochemistry , gene , dimer , physics , organic chemistry , quantum mechanics , artificial intelligence , magnetic field , computer science
The structure of human brain CutA1 ( Hs CutA1) has been determined using diffraction data to 2.05 Å resolution. Hs CutA1 has been implicated in the anchoring of acetylcholinesterase in neuronal cell membranes, while its bacterial homologue Escherichia coli CutA1 is involved in copper tolerance. Additionally, the structure of Hs CutA1 bears similarity to that of the signal transduction protein PII, which is involved in regulation of nitrogen metabolism. Although several crystal structures of CutA1 from various sources with different rotation angles and degrees of interaction between trimer interfaces have been reported, the specific functional role of CutA1 is still unclear. In this study, the X‐ray structure of Hs CutA1 was determined in space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 68.69, b = 88.84, c = 125.33 Å and six molecules per asymmetric unit. Hs CutA1 is a trimeric molecule with intertwined antiparallel β‐strands; each subunit has a molecular weight of 14.6 kDa and contains 135 amino‐acid residues. In order to obtain clues to the possible function of Hs CutA1, its crystal structure was compared with those of other CutA1 and PII proteins.