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PDBsum entry 2mqh
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DNA binding protein
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PDB id
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2mqh
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References listed in PDB file
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Key reference
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Title
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Solution structure of the RNA-Binding cold-Shock domain of the chlamydomonas reinhardtii nab1 protein and insights into RNA recognition.
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Authors
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A.L.Sawyer,
M.J.Landsberg,
I.L.Ross,
O.Kruse,
M.Mobli,
B.Hankamer.
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Ref.
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Biochem J, 2015,
469,
97.
[DOI no: ]
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PubMed id
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Abstract
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Light-harvesting complex (LHC) proteins are among the most abundant proteins on
Earth and play critical roles in photosynthesis, both in light capture and in
photoprotective mechanisms. The Chlamydomonas reinhardtii nucleic acid-binding
protein 1 (NAB1) is a negative regulator of LHC protein translation. Its
N-terminal cold-shock domain (CSD) binds to a 13-nt element [CSD consensus
sequence (CSDCS)] found in the mRNA of specific LHC proteins associated with
Photosystem II (PSII), an interaction which regulates LHC expression and,
consequently, PSII-associated antenna size, structure and function. In the
present study, we elucidated the solution structure of the NAB1 CSD as
determined by heteronuclear NMR. The CSD adopts a characteristic five-stranded
anti parallel β-barrel fold. Upon addition of CSDCS RNA, a large number of NMR
chemical shift perturbations were observed, corresponding primarily to
surface-exposed residues within the highly conserved β2- and β3-strands in the
canonical RNA-binding region, but also to residues on β-strand 5 extending the
positive surface patch and the overall RNA-binding site. Additional chemical
shift perturbations that accompanied RNA binding involved buried residues,
suggesting that transcript recognition is accompanied by conformational change.
Our results indicate that NAB1 associates with RNA transcripts through a
mechanism involving its CSD that is conserved with mechanisms of
sequence-specific nucleic acid recognition employed by ancestrally related
bacterial cold-shock proteins (CSPs).
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Secondary reference #1
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Title
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Cloning, Purification, Crystallization and 1.57 å resolution X-Ray data analysis of amsi, The tyrosine phosphatase controlling amylovoran biosynthesis in the plant pathogen erwinia amylovora.
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Authors
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S.Benini,
L.Caputi,
M.Cianci.
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Ref.
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Acta Crystallogr F Struct Biol Commun, 2014,
70,
1693-1696.
[DOI no: ]
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PubMed id
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