1HQZ

Cofilin homology domain of a yeast actin-binding protein ABP1P

Summary for 1HQZ

• Entry DOI: 10.2210/pdb1hqz/pdb
• Descriptor: ACTIN-BINDING PROTEIN (2 entities in total)
• Functional Keywords: cofilin homology domain, actin binding, new york sgx research center for structural genomics, nysgxrc, structural genomics, psi, protein structure initiative, structural protein
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 9
• Total formula weight: 140745.61

Authors

Strokopytov, B.V.,Fedorov, A.A.,Mahoney, N.,Drubin, D.G.,Almo, S.C.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2000-12-20, release date: 2001-12-21, Last modification date: 2023-08-09)

Primary citation

Strokopytov, B.V.,Fedorov, A.,Mahoney, N.M.,Kessels, M.,Drubin, D.G.,Almo, S.C.
Phased translation function revisited: structure solution of the cofilin-homology domain from yeast actin-binding protein 1 using six-dimensional searches.
Acta Crystallogr.,Sect.D, 61:285-293, 2005

PubMed Abstract: A modified molecular-replacement method is described that makes use of six-dimensional searches and the phased translation function, providing a systematic examination of all possible search-model orientations in an experimental electron-density map. As an example, the structure solution of the cofilin-homology domain of the Saccharomyces cerevisiae actin-binding protein 1 (ABP1) is presented in detail. Additional examples are presented in which these tools have significantly aided structure solutions in a variety of contexts. These results suggest that this approach might be of widespread utility for challenging structures involving weak phase information, complex asymmetric units and search models with weak structural homology. Furthermore, this approach supports an exhaustive molecular-replacement strategy in cases where an appropriate search model cannot readily be identified on the basis of sequence homology. The fully automated web-based implementation of this phased translation function is described.

PubMed: 15735338
DOI: 10.1107/S0907444904033037

Experimental method

X-RAY DIFFRACTION (2.1 Å)