1p2x | pdb_00001p2x
CRYSTAL STRUCTURE OF THE CALPONIN-HOMOLOGY DOMAIN OF RNG2 FROM SCHIZOSACCHAROMYCES POMBE
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Overview
Schizosaccharomyces pombe Rng2 is an IQGAP protein that is essential for, the assembly of an actomyosin ring during cytokinesis. Rng2 contains an, amino-terminal calponin-homology (CH) domain, 11 IQ repeats and a, RasGAP-homology domain. CH domains are known mainly for their ability to, bind F-actin, although they have other ligands in vivo and there are only, few examples of actin-binding single CH domains. The structures of several, CH domains have already been reported, but this is only the third report, of an actin-binding protein that contains a single CH domain (the, structures of calponin and EB1 have been reported previously). The 2.21 A, resolution crystal structure of the amino-terminal 190 residues of Rng2, from Br- and Hg-derivatives includes 40 residues (150-190), carboxyl-terminal to the CH domain that resemble neither the extended, conformation seen in utrophin, nor the compact conformation seen in, fimbrin, although residues 154-160 form an unstructured coil which adopts, a substructure similar to dystrophin residues 240-246 in the, carboxyl-terminal portion of the CH2 domain. This region wraps around the, stretch of residues that would be equivalent to the proposed actin-binding, site ABS1 and ABS2 from dystrophin. This distinctive feature is absent, from previously published CH-domain structures. Another feature revealed, by comparing the two derivatives is the presence of two loop conformations, between Tyr92 and Arg99.
About this Structure
1P2X is a Single protein structure of sequence from Schizosaccharomyces pombe with BR as ligand. Full crystallographic information is available from OCA.
Reference
Structure, crystal packing and molecular dynamics of the calponin-homology domain of Schizosaccharomyces pombe Rng2., Wang CH, Balasubramanian MK, Dokland T, Acta Crystallogr D Biol Crystallogr. 2004 Aug;60(Pt 8):1396-403. Epub 2004, Jul 21. PMID:15272162
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