ArticleActa crystallographica. Section F, Structural biology and crystallization communications2008
Structure of putative CutA1 from Homo sapiens determined at 2.05 A resolution.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 4 citations in OpenAlex.
- Structure of a CutA1 divalent-cation tolerance protein from Cryptosporidium parvum, the protozoal parasite responsible for cryptosporidiosis.Acta crystallographica. Section F, Structural biology communications · 2015Article
- The structures of the CutA1 proteins from Thermus thermophilus and Pyrococcus horikoshii: characterization of metal-binding sites and metal-induced assembly.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Crystal structure of stable protein CutA1 from psychrotrophic bacterium Shewanella sp. SIB1.Journal of synchrotron radiation · 2011Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The structure of human brain CutA1 (HsCutA1) has been determined using diffraction data to 2.05 A resolution. HsCutA1 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 HsCutA1 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 HsCutA1 was determined in space group P2(1)2(1)2(1), with unit-cell parameters a = 68.69, b = 88.84, c = 125.33 A and six molecules per asymmetric unit. HsCutA1 is a trimeric molecule with intertwined antiparallel beta-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 HsCutA1, its crystal structure was compared with those of other CutA1 and PII proteins.
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