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PDBsum entry 3d7a
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Unknown function
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PDB id
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3d7a
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Contents |
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* Residue conservation analysis
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DOI no:
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Proteins
74:256-260
(2009)
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PubMed id:
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Crystal structure of the DUF54 family protein PH1010 from hyperthermophilic archaea Pyrococcus horikoshii OT3.
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K.Miyazono,
M.Shirokane,
Y.Sawano,
M.Tanokura.
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ABSTRACT
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Selected figure(s)
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Figure 1.
Figure 1. The structure of PH1010. (A) Ribbon diagram of the
monomer structure of PH1010 (Chain A). Color-coding runs from
blue in the N-terminal region to red in the C-terminal region.
Secondary structure assignments are labeled on the ribbon model.
(B) The dimer structure of PH1010. One subunit is colored
according to its secondary structure (helices, cyan; strands,
pink) and the other is colored gray. The locations of Thr17 and
the loop 4-
6
are indicated by red and blue circles, respectively. (C)
Hydrogen-bond network observed in the dimerization interface.
Residues forming the hydrogen-bond network are shown by a stick
model. (D) The electrostatic potential diagram of the slightly
twisted -sheet
side of PH1010 and ribosomal protein L5. Positive and negative
potentials are represented by blue and red, respectively. The
maximum and the minimum values of the electrostatic potentials
are ±5 kT/e, respectively.
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Figure 2.
Figure 2. Comparison with other structures. (A) Superposition
of PH1010 (cyan), 50S ribosomal protein L5 (gray), and SSO1042
(red). (B) Amino acid sequence alignment of PH1010 and other
DUF54 family proteins: SSO1042 (PDB ID: 2NWU), MJ1564 (PDB ID:
2PZZ), Af2318 (PDB ID: 2OGK), and SSO0741 (PDB ID: 2NRQ). The
secondary structure assignment for PH1010 is indicated by
helices ( -helices)
and arrows ( -strands).
Residues forming the dimerization interface are indicated by an
asterisk.
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The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2009,
74,
256-260)
copyright 2009.
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');
}
}
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