PDBsum entry 4wia

Atp-binding protein

PDB id: 4wia

Contents

Protein chains

229 a.a.

Ligands

SO4 ×13

GOL

Waters ×70

PDB id:

4wia

Name:

Atp-binding protein

Title:

Crystal structure of flagellar accessory protein flah from methanocaldococcus jannaschii

Structure:

Putative flagella-related protein h. Chain: a, b, c. Engineered: yes

Source:

Methanocaldococcus jannaschii dsm 2661. Organism_taxid: 243232. Gene: flah, mj0899. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.20Å R-factor: 0.207 R-free: 0.233

Authors:

V.A.Meshcheryakov,M.Wolf

Key ref:

V.A.Meshcheryakov and M.Wolf (2016). Crystal structure of the flagellar accessory protein FlaH of Methanocaldococcus jannaschii suggests a regulatory role in archaeal flagellum assembly. Protein Sci, 25, 1147-1155. PubMed id: 27060465 DOI: 10.1002/pro.2932

Date:

25-Sep-14 Release date: 07-Oct-15

Protein chains

Q58309  (FLAH_METJA) -  Archaeal flagellar ATP-binding protein FlaH from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

Seq: 233 a.a.

Struc: 229 a.a.

DOI no: 10.1002/pro.2932

Protein Sci 25:1147-1155 (2016)

PubMed id: 27060465

Crystal structure of the flagellar accessory protein FlaH of Methanocaldococcus jannaschii suggests a regulatory role in archaeal flagellum assembly.

V.A.Meshcheryakov, M.Wolf.

ABSTRACT

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.