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PDBsum entry 4hzb
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115 a.a.
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122 a.a.
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116 a.a.
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PDB id:
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Hydrolase
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Title:
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Crystal structure of the type vi semet effector-immunity complex tae3- tai3 from ralstonia pickettii
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Structure:
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Putative cytoplasmic protein. Chain: a, d. Synonym: toxin protein. Engineered: yes. Putative periplasmic protein. Chain: b, c, e, f. Synonym: antitoxin protein. Engineered: yes
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Source:
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Ralstonia pickettii. Organism_taxid: 428406. Strain: 12d. Gene: rpic12d_3261. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: rpic12d_3260. Expression_system_taxid: 562
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Resolution:
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2.60Å
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R-factor:
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0.216
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R-free:
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0.271
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Authors:
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C.Dong,H.Zhang,Z.Q.Gao,Y.H.Dong
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Key ref:
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C.Dong
et al.
(2013).
Structural insights into the inhibition of type VI effector Tae3 by its immunity protein Tai3.
Biochem J,
454,
59-68.
PubMed id:
DOI:
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Date:
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15-Nov-12
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Release date:
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21-Aug-13
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PROCHECK
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Headers
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References
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C6BHF2
(C6BHF2_RALP1) -
Putative cytoplasmic protein from Ralstonia pickettii (strain 12D)
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Seq:
Struc:
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119 a.a.
115 a.a.
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DOI no:
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Biochem J
454:59-68
(2013)
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PubMed id:
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Structural insights into the inhibition of type VI effector Tae3 by its immunity protein Tai3.
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C.Dong,
H.Zhang,
Z.Q.Gao,
W.J.Wang,
Z.She,
G.F.Liu,
Y.Q.Shen,
X.D.Su,
Y.H.Dong.
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ABSTRACT
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The recently described T6SS (type VI secretion system) acts as a needle that
punctures the membrane of the target cells to deliver effector proteins.
Type VI amidase effectors can be classified into four divergent families
(Tae1-Tae4). These effectors are secreted into the periplasmic space of
neighbouring cells via the T6SS and subsequently rupture peptidoglycan. However,
the donor cells are protected from damage because of the presence of their
cognate immunity proteins [Tai1 (type VI amidase immunity 1)-Tai4]. In the
present paper, we describe the structure of Tae3 in complex with Tai3. The
Tae3-Tai3 complex exists as a stable heterohexamer, which is composed of two
Tae3 molecules and two Tai3 homodimers (Tae3-Tai34-Tae3). Tae3 shares a common
NlpC/P60 fold, which consists of N-terminal and C-terminal subdomains.
Structural analysis indicates that two unique loops around the catalytic cleft
adopt a closed conformation, resulting in a narrow and extended groove involved
in the binding of the substrate. The inhibition of Tae3 is attributed to the
insertion of the Ω-loop (loop of α3-α4) of Tai3 into the catalytic groove.
Furthermore, a cell viability assay confirmed that a conserved motif
(Gln-Asp-Xaa) in Tai3 members may play a key role in the inhibition process.
Taken together, the present study has revealed a novel inhibition mechanism and
provides insights into the role played by T6SS in interspecific competition.
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