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PDBsum entry 2zfh
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Structural genomics, unknown function
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PDB id
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2zfh
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Structural genomics, unknown function
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Title:
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Crystal structure of putative cuta1 from homo sapiens at 2.05a resolution
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Structure:
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Cuta. Chain: a, b, c, d, e, f. Synonym: brain acetylcholinesterase putative membrane anchor, acetylcholinesterase-associated protein. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: cuta, achap, c6orf82. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.05Å
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R-factor:
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0.221
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R-free:
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0.265
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Authors:
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B.Bagautdinov,K.Yutani,Riken Structural Genomics/proteomics Initiative (Rsgi)
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Key ref:
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B.Bagautdinov
et al.
(2008).
Structure of putative CutA1 from Homo sapiens determined at 2.05 A resolution.
Acta Crystallogr Sect F Struct Biol Cryst Commun,
64,
351-357.
PubMed id:
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Date:
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07-Jan-08
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Release date:
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22-Jan-08
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PROCHECK
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Headers
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References
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O60888
(CUTA_HUMAN) -
Protein CutA from Homo sapiens
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Seq:
Struc:
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179 a.a.
109 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Acta Crystallogr Sect F Struct Biol Cryst Commun
64:351-357
(2008)
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PubMed id:
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Structure of putative CutA1 from Homo sapiens determined at 2.05 A resolution.
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B.Bagautdinov,
Y.Matsuura,
S.Bagautdinova,
N.Kunishima,
K.Yutani.
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ABSTRACT
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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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