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PDBsum entry 4pls
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Peptide binding protein
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PDB id
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4pls
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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 structures of designed armadillo repeat proteins: implications of construct design and crystallization conditions on overall structure.
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Authors
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C.Reichen,
C.Madhurantakam,
A.Plückthun,
P.R.Mittl.
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Ref.
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Protein Sci, 2014,
23,
1572-1583.
[DOI no: ]
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PubMed id
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Abstract
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Designed armadillo repeat proteins (dArmRP) are promising modular proteins for
the engineering of binding molecules that recognize extended polypeptide chains.
We determined the structure of a dArmRP containing five internal repeats and 3rd
generation capping repeats in three different states by X-ray crystallography:
without N-terminal His6 -tag and in the presence of calcium (YM5 A/Ca(2+) ),
without N-terminal His6 -tag and in the absence of calcium (YM5 A), and with
N-terminal His6 -tag and in the presence of calcium (His-YM5 A/Ca(2+) ). All
structures show different quaternary structures and superhelical parameters.
His-YM5 A/Ca(2+) forms a crystallographic dimer, which is bridged by the His6
-tag, YM5 A/Ca(2+) forms a domain-swapped tetramer, and only in the absence of
calcium and the His6 -tag, YM5 A forms a monomer. The changes of superhelical
parameters are a consequence of calcium binding, because calcium ions interact
with negatively charged residues, which can also participate in the modulation
of helix dipole moments between adjacent repeats. These observations are
important for further optimizations of dArmRPs and provide a general
illustration of how construct design and crystallization conditions can
influence the exact structure of the investigated protein.
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