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PDBsum entry 5b0o
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Hydrolase/motor protein
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PDB id
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5b0o
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Contents |
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445 a.a.
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(+ 0 more)
135 a.a.
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126 a.a.
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127 a.a.
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PDB id:
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| Name: |
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Hydrolase/motor protein
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Title:
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Structure of the flih-flii complex
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Structure:
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Flagellum-specific atp synthase. Chain: a, b, c, d. Engineered: yes. Flagellar assembly protein flih. Chain: e, f, g, h, i, j, k, l. Fragment: unp residues 99-235. Engineered: yes
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Source:
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Salmonella typhimurium (strain lt2 / sgsc1412 / atcc 700720). Organism_taxid: 99287. Strain: lt2 / sgsc1412 / atcc 700720. Gene: flii, fla aiii, flac, stm1972. Expressed in: escherichia coli. Expression_system_taxid: 562. Salmonella typhimurium. Gene: flih, fla aii.3, fla biii, stm1971.
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Resolution:
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3.00Å
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R-factor:
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0.220
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R-free:
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0.270
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Authors:
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K.Imada,Y.Uchida,M.Kinoshita,K.Namba,T.Minamino
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Key ref:
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K.Imada
et al.
(2016).
Insight into the flagella type III export revealed by the complex structure of the type III ATPase and its regulator.
Proc Natl Acad Sci U S A,
113,
3633-3638.
PubMed id:
DOI:
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Date:
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02-Nov-15
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Release date:
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23-Mar-16
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PROCHECK
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Headers
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References
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P26465
(FLII_SALTY) -
Flagellum-specific ATP synthase from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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Seq:
Struc:
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456 a.a.
445 a.a.
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P15934
(FLIH_SALTY) -
Flagellar assembly protein FliH from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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Seq:
Struc:
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235 a.a.
135 a.a.
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Enzyme class 2:
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Chains A, B, C, D:
E.C.7.1.2.2
- H(+)-transporting two-sector ATPase.
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Reaction:
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ATP + H2O + 4 H+(in) = ADP + phosphate + 5 H+(out)
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ATP
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+
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H2O
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+
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4
×
H(+)(in)
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=
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ADP
Bound ligand (Het Group name = )
corresponds exactly
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+
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phosphate
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+
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5
×
H(+)(out)
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Enzyme class 3:
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Chains E, F, G, H, I, J, K, L:
E.C.?
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Proc Natl Acad Sci U S A
113:3633-3638
(2016)
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PubMed id:
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Insight into the flagella type III export revealed by the complex structure of the type III ATPase and its regulator.
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K.Imada,
T.Minamino,
Y.Uchida,
M.Kinoshita,
K.Namba.
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ABSTRACT
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FliI and FliJ form the FliI6FliJ ATPase complex of the bacterial flagellar
export apparatus, a member of the type III secretion system. The FliI6FliJ
complex is structurally similar to the α3β3γ complex of F1-ATPase. The FliH
homodimer binds to FliI to connect the ATPase complex to the flagellar base, but
the details are unknown. Here we report the structure of the homodimer of a
C-terminal fragment of FliH (FliHC2) in complex with FliI. FliHC2shows an
unusually asymmetric homodimeric structure that markedly resembles the
peripheral stalk of the A/V-type ATPases. The FliHC2-FliI hexamer model reveals
that the C-terminal domains of the FliI ATPase face the cell membrane in a way
similar to the F/A/V-type ATPases. We discuss the mechanism of flagellar ATPase
complex formation and a common origin shared by the type III secretion system
and the F/A/V-type ATPases.
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