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Title
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Crystal packing induces a conformational change in profilin-I from Acanthamoeba castellanii.
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Authors
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S.Liu,
A.A.Fedorov,
T.D.Pollard,
E.E.Lattman,
S.C.Almo,
K.A.Magnus.
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Ref.
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J Struct Biol, 1998,
123,
22-29.
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PubMed id
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Abstract
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Profilin-I from Acanthamoeba castellanii is a 13-kDa protein that binds actin
and poly-l-proline. The native protein has been crystallized in two different
but closely related forms. The second form proved more amenable to
three-dimensional structural determination using heavy-atom isomorphous methods
to obtain crystallographic phase information. We used the second crystal
structure as a test molecule in the molecular replacement procedure to determine
the structure of the first crystal form of profilin-I. More residues participate
in crystal lattice contacts in the first crystal form than in the second. The
two crystal forms differ significantly in the C-terminal helix that interacts
with actin and in the loop preceding this helix. Coordinates of some main chain
atoms here differ by about 1.0 A, and side chain atoms differ by more than 2.0 A.
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