Molecular packing in profilin: actin crystals and its implications.
Analysis of profilin: actin crystals reveals an extensive intermolecular network, rather than a discrete "monomeric complex", comprising stacked actin ribbons held in place by columns of profilin molecules, wedged in between neighboring actin subunits and running perpendicular to the ribbons. Comparison with data from electron microscopy, X-ray diffraction, spectroscopy, and biochemistry of actin suggests that a simple transformation relates the ribbon to f-actin. The crystals exhibit unusual polymorphic properties, which strengthens the view that movements within the actin monomer are important for force generation.
Schutt
C E
CE
MRC Laboratory of Molecular Biology, Cambridge, England.
Lindberg
U
U
Myslik
J
J
Strauss
N
N
D000199:Actins / Q000032:analysis* / Q000648:ultrastructure; D000255:Adenosine Triphosphate / Q000378:metabolism; D003285:Contractile Proteins; D003460:Crystallization; D003461:Crystallography; D008840:Microfilament Proteins / Q000032:analysis*; D009119:Muscle Contraction; D051304:Profilins; D011487:Protein Conformation
D000199:Actins; D003285:Contractile Proteins; D008840:Microfilament Proteins; D051304:Profilins; D000255:Adenosine Triphosphate