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PDBsum entry 2fo7
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De novo protein
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PDB id
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2fo7
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References listed in PDB file
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Key reference
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Title
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Structure and stability of designed tpr protein superhelices: unusual crystal packing and implications for natural tpr proteins.
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Authors
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T.Kajander,
A.L.Cortajarena,
S.Mochrie,
L.Regan.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2007,
63,
800-811.
[DOI no: ]
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PubMed id
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Abstract
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The structure and stability of repeat proteins has been little studied in
comparison to the properties of the more familiar globular proteins. Here, the
structure and stability of designed tetratricopeptide-repeat (TPR) proteins is
described. The TPR is a 34-amino-acid motif which adopts a helix-turn-helix
structure and occurs as tandem repeats. The design of a consensus TPR motif
(CTPR) has previously been described. Here, the crystal structures and
stabilities of proteins that contain eight or 20 identical tandem repeats of the
CTPR motif (CTPR8 and CTPR20) are presented. Both CTPR8 and CTPR20 adopt a
superhelical overall structure. The structures of the different-length CTPR
proteins are compared with each other and with the structures of natural TPR
domains. Also, the unusual and perhaps unique crystal-packing interactions
resulting in pseudo-infinite crystalline superhelices observed in the different
crystal forms of CTPR8 and CTPR20 are discussed. Finally, it is shown that the
thermodynamic behavior of CTPR8 and CTPR20 can be predicted from the behavior of
other TPRs in this series using an Ising model-based analysis. The designed
protein series CTPR2-CTPR20 covers the natural size repertoire of TPR domains
and as such is an excellent model system for natural TPR proteins.
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Figure 7.
Figure 7 Schematic representation of the crystal-packing
interactions between superhelical molecules. (a) As an example,
in P4[1]2[1]2 there are two repeats (numbered 1-8) within the
asymmetric unit (indicated as AU; red box). For this arrangement
there are eight equally possible two-repeat arrangements for the
asymmetric unit. (b) Schematic illustration of the stacking of
helices between repeats of individual molecules. The first
A-helix of the next molecule must always pack against the last
repeat of the previous molecule and therefore the C-terminal
capping helix must be displaced. (c) Ribbon representation of
the superhelical stacking with each single repeat coloured
yellow or blue.
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Figure 8.
Figure 8 Alignment of repeats 3-10 of the TPR domain of OGT
(red) with the tetragonal crystal structure of CTPR8 (blue).
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2007,
63,
800-811)
copyright 2007.
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Secondary reference #1
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Title
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A new folding paradigm for repeat proteins.
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Authors
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T.Kajander,
A.L.Cortajarena,
E.R.Main,
S.G.Mochrie,
L.Regan.
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Ref.
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J Am Chem Soc, 2005,
127,
10188-10190.
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PubMed id
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