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PDBsum entry 4wia
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Atp-binding protein
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PDB id
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4wia
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the flagellar accessory protein flah of methanocaldococcus jannaschii suggests a regulatory role in archaeal flagellum assembly.
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Authors
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V.A.Meshcheryakov,
M.Wolf.
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Ref.
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Protein Sci, 2016,
25,
1147-1155.
[DOI no: ]
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PubMed id
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Abstract
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Archaeal flagella are unique structures that share functional similarity with
bacterial flagella, but are structurally related to bacterial type IV pili. The
flagellar accessory protein FlaH is one of the conserved components of the
archaeal motility system. However, its function is not clearly understood. Here,
we present the 2.2 Å resolution crystal structure of FlaH from the
hyperthermophilic archaeon, Methanocaldococcus jannaschii. The protein has a
characteristic RecA-like fold, which has been found previously both in archaea
and bacteria. We show that FlaH binds to immobilized ATP-however, it lacks
ATPase activity. Surface plasmon resonance analysis demonstrates that ATP
affects the interaction between FlaH and the archaeal motor protein FlaI. In the
presence of ATP, the FlaH-FlaI interaction becomes significantly weaker. A
database search revealed similarity between FlaH and several DNA-binding
proteins of the RecA superfamily. The closest structural homologs of FlaH are
KaiC-like proteins, which are archaeal homologs of the circadian clock protein
KaiC from cyanobacteria. We propose that one of the functions of FlaH may be the
regulation of archaeal motor complex assembly.
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