Structure of putative CutA1 from Homo sapiens determined at 2.05 A resolution.

Structure of putative CutA1 from Homo sapiens determined at 2.05 A resolution. Research Abstract Details 

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Structure of putative CutA1 from Homo sapiens determined at 2.05 A resolution. Abstract Text:

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.

Structure of putative CutA1 from Homo sapiens determined at 2.05 A resolution. Publishing Authors By Initials

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Structure of putative CutA1 from Homo sapiens determined at 2.05 A resolution. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Acta crystallographica. Section F, Structural biol

VOLUME: 64

Page Numbers: 351-7

Journal Abbreviation: Acta Crystallogr. Sect. F Stru

ISSN: 1744-3091

DAY: 30

MONTH: 04

YEAR: 2008

Structure of putative CutA1 from Homo sapiens determined at 2.05 A resolution. Information

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LANGUAGE: eng

NlmUniqueID: 101226117

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AFFILIATION: Protein Structure Analysis Team, RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan. bagautdi@spring8.or.jp

Country: England

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MEDLINETA: Acta Crystallogr Sect F Struct

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