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PDBsum entry 2nx8
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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 tRNA-Specific adenosine deaminase from streptococcus pyogenes.
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Authors
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W.H.Lee,
Y.K.Kim,
K.H.Nam,
A.Priyadarshi,
E.H.Lee,
E.E.Kim,
Y.H.Jeon,
C.Cheong,
K.Y.Hwang.
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Ref.
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Proteins, 2007,
68,
1016-1019.
[DOI no: ]
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PubMed id
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Abstract
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No abstract given.
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Figure 1.
Figure 1. (A) Overall structure A schematic ribbon diagram of
the overall structure of the tRNA-specific adenosine deaminase
(residues 5-173) from S. pyogenes (spTad A). The N- and
C-termini of the protein are labeled, and the helices and sheets
are numbered. Zn (II) and the phosphate ion are shown in gray
sphere and ball-and-stick models, respectively. (B)
Superimposition of spTadA and other proteins. The overall
structure of spTadA is superimposed on other TadA proteins in a
ribbon model representation. The blue, yellow, red and green
colors are shown to S. pyogenes TadA, A. aeolicus TadA (1WWR),
E. coli TadA (1Z3A), and Staphylococcus aureus TadA (2B3J),
respectively. The red circles are shown in the main differences.
(C) Comparison of active sites between spTadA and
saTadA-complexed with RNA. A detailed depiction of the
interacting residues of the active site compared to
Staphylococcus aureus Tad A (saTadA) is shown by ball-and-stick
models. In saTadA, the His residue has the  -
interaction
with PURINE RIBOSIDE-5  -MONOPHOSPHATE
(C[10] H[13] N[4] O[7] P) (PR5). Green residues are spTadA,
yellow residues the saTad A (2B3J), blue the phosphate ion,
PO[4]^- (spTad), and red is PR5 (2B3J). (D) The dimer interface
of spTadA. The monomers interact with each other symmetrically.
The residues participated in forming the interfaces are shown as
ball-and-stick models and the interaction with another monomer.
The hydrogen bonding and hydrophobic interactions are major
forces in forming the dimer interface.
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The above figure is
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2007,
68,
1016-1019)
copyright 2007.
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