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PDBsum entry 1jch
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Ribosome inhibitor, hydrolase
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PDB id
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1jch
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Contents |
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* Residue conservation analysis
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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 colicin e3: implications for cell entry and ribosome inactivation.
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Authors
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S.Soelaiman,
K.Jakes,
N.Wu,
C.Li,
M.Shoham.
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Ref.
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Mol Cell, 2001,
8,
1053-1062.
[DOI no: ]
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PubMed id
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Abstract
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Colicins kill E. coli by a process that involves binding to a surface receptor,
entering the cell, and, finally, intoxicating it. The lethal action of colicin
E3 is a specific cleavage in the ribosomal decoding A site. The crystal
structure of colicin E3, reported here in a binary complex with its immunity
protein (IP), reveals a Y-shaped molecule with the receptor binding domain
forming a 100 A long stalk and the two globular heads of the translocation
domain (T) and the catalytic domain (C) comprising the two arms. Active site
residues are D510, H513, E517, and R545. IP is buried between T and C. Rather
than blocking the active site, IP prevents access of the active site to the
ribosome.
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Figure 1.
Figure 1. Schematic Representation of the Mechanism of
Action of Colicin E3T, translocation domain; R, receptor binding
domain; C, catalytic domain; IP, immunity protein to colicin E3.
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Figure 2.
Figure 2. Ribbon Diagrams(A) The colicin E3-IP complex is Y
shaped with dimensions of 75 × 135 × 45 Å.(B)
Close-up of the jellyroll structure of the translocation domain
in the same orientation as in (A). The three β sheets are shown
in red, blue, and yellow. The β strands are numbered
consecutively from the N terminus. The β barrel is flanked by
two α-helical stretches. The second and longer α helix ends
with P315, which causes a kink in the helix and leads directly
into the helical receptor binding domain.(C) Close-up of the
catalytic domain and the IP. The C domain is shown in gray and
the IP in red. Catalytic residues are shown in ball-and-stick.
This orientation shows that the two β sheets are roughly
perpendicular to each other.
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2001,
8,
1053-1062)
copyright 2001.
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