1p2x
From Proteopedia
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CRYSTAL STRUCTURE OF THE CALPONIN-HOMOLOGY DOMAIN OF RNG2 FROM SCHIZOSACCHAROMYCES POMBE
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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