1P2X
CRYSTAL STRUCTURE OF THE CALPONIN-HOMOLOGY DOMAIN OF RNG2 FROM SCHIZOSACCHAROMYCES POMBE
Summary for 1P2X
| Entry DOI | 10.2210/pdb1p2x/pdb |
| Descriptor | Ras GTPase-activating-like protein, BROMIDE ION (3 entities in total) |
| Functional Keywords | 4 helices, bundle, protein binding |
| Biological source | Schizosaccharomyces pombe (fission yeast) |
| Cellular location | Cytoplasm, cytoskeleton: O14188 |
| Total number of polymer chains | 1 |
| Total formula weight | 19355.15 |
| Authors | Wang, C.-H.,Balasubramanian, M.K.,Dokland, T. (deposition date: 2003-04-16, release date: 2004-06-08, Last modification date: 2024-02-14) |
| Primary citation | Wang, C.H.,Balasubramanian, M.K.,Dokland, T. Structure, crystal packing and molecular dynamics of the calponin-homology domain of Schizosaccharomyces pombe Rng2. Acta Crystallogr.,Sect.D, 60:1396-1403, 2004 Cited by PubMed Abstract: 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. PubMed: 15272162DOI: 10.1107/S0907444904012983 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.21 Å) |
Structure validation
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