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PDBsum entry 2aq5
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Structural protein
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PDB id
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2aq5
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References listed in PDB file
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Key reference
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Title
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The crystal structure of murine coronin-1: a regulator of actin cytoskeletal dynamics in lymphocytes.
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Authors
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B.A.Appleton,
P.Wu,
C.Wiesmann.
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Ref.
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Structure, 2006,
14,
87-96.
[DOI no: ]
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PubMed id
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Abstract
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Mammalian coronin-1 is preferentially expressed in hematopoietic cells and plays
a poorly understood role in the dynamic reorganization of the actin
cytoskeleton. Sequence analysis of coronin-1 revealed five WD40 repeats that
were predicted to form a beta propeller. They are followed by a 130 residue
extension and a 30 residue leucine zipper domain that is responsible for
multimerization of the protein. Here, we present the crystal structure of murine
coronin-1 without the leucine zipper at 1.75 A resolution. Coronin-1 forms a
seven-bladed beta propeller composed of the five predicted WD40 repeats and two
additional blades that lack any homology to the canonical WD40 motif. The
C-terminal extension adopts an extended conformation, packs tightly against the
bottom surface of the propeller, and is likely to be required for the structural
stability of the propeller. Analysis of charged and conserved surface residues
delineate possible binding sites for F-actin on the beta propeller.
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Figure 1.
Figure 1. The Overall Structure of Murine Coronin-1
(A) Ribbon diagrams of coronin-1 showing the "top" (left) and
"bottom" (right) side of the b propeller. The structure can be
divided into an N-terminal seven-bladed b propeller (residues
8-352; colored blue, yellow, and green) and a C-terminal
extension (residues 353-402; colored red). The last ordered
residues of the N and C termini are marked with an "NT" and
"CT," respectively. The individual blades are numbered from one
to seven; the strands in each blade are named A-D and are
labeled in blade 4.
(B) The "side" view highlights the
C-terminal extension (red) tightly packing against the "bottom"
surface of the propeller. The structure lacks the C-terminal
leucine zipper responsible for multimerization (Gatfield et al.,
2005 and Oku et al., 2005), and, accordingly, the protein is
monomeric. All figures were generated with PyMol (DeLano, 2002).
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2006,
14,
87-96)
copyright 2006.
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