1hlu
From Proteopedia
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STRUCTURE OF BOVINE BETA-ACTIN-PROFILIN COMPLEX WITH ACTIN BOUND ATP PHOSPHATES SOLVENT ACCESSIBLE
Overview
The structure of an "open state" of crystalline profilin:beta-actin has, been solved to 2.65 A by X-ray crystallography. The open-state crystals, in 1.8 M potassium phosphate, have an expanded unit cell dimension in the, c direction of 185.7 A compared with 171.9 A in the previously solved, ammonium sulphate-stabilized "tight-state" structure. The unit cell change, between the open and the tight states is accompanied by large subdomain, movements in actin. Furthermore, the nucleotide in the open state is, significantly more exposed to solvent, and local conformational changes in, the hydrophobic pocket surrounding cysteine 374 occur during the, transition to the tight state. Significant changes were observed at the N, terminus and in the DNase-I binding loop. Neither the structure of, ... [(full description)]
About this Structure
1HLU is a [Protein complex] structure of sequences from [Bos taurus] with CA, ACE and ATP as [ligands]. The following page contains interesting information on the relation of 1HLU with [Actin]. Structure known Active Sites: CAT and NUC. Full crystallographic information is available from [OCA].
Reference
The structure of an open state of beta-actin at 2.65 A resolution., Chik JK, Lindberg U, Schutt CE, J Mol Biol. 1996 Nov 8;263(4):607-23. PMID:8918942
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