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PDBsum entry 5lb5
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References listed in PDB file
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Key reference
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Title
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Insights into the recq helicase mechanism revealed by the structure of the helicase domain of human recql5.
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Authors
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J.A.Newman,
H.Aitkenhead,
P.Savitsky,
O.Gileadi.
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Ref.
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Nucleic Acids Res, 2017,
45,
4231-4243.
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PubMed id
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Abstract
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RecQ helicases are important maintainers of genome integrity with distinct roles
in almost every cellular process requiring access to DNA. RECQL5 is one of five
human RecQ proteins and is particularly versatile in this regard, forming
protein complexes with a diverse set of cellular partners in order to coordinate
its helicase activity to various processes including replication, recombination
and DNA repair. In this study, we have determined crystal structures of the core
helicase domain of RECQL5 both with and without the nucleotide ADP in two
distinctly different ('Open' and 'Closed') conformations. Small angle X-ray
scattering studies show that the 'Open' form of the protein predominates in
solution and we discuss implications of this with regards to the RECQL5
mechanism and conformational changes. We have measured the ATPase, helicase and
DNA binding properties of various RECQL5 constructs and variants and discuss the
role of these regions and residues in the various RECQL5 activities. Finally, we
have performed a systematic comparison of the RECQL5 structures with other RecQ
family structures and based on these comparisons we have constructed a model for
the mechano-chemical cycle of the common catalytic core of these helicases.
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