1olo

From Proteopedia

Revision as of 15:34, 29 October 2007

HEXAMERIC REPLICATIVE DNA HELICASE REPA FROM PLASMID RSF1010- CUBIC CRYSTAL STRUCTURE

Overview

In the known monoclinic crystals the 3-dimensional structure of the, hexameric, replicative helicase RepA encoded by plasmid RSF1010 shows, 6-fold rotational symmetry. In contrast, in the cubic crystal form at 2.55, A resolution described here RepA has 3-fold symmetry and consists of a, trimer of dimers. To study structure-function relationships, a series of, repA deletion mutants and mutations yielding single amino acid exchanges, were constructed and the respective gene products were analyzed in vivo, and in vitro. Hexamerization of RepA occurs via the N-terminus and is, required for NTP hydrolysis. The C-terminus is essential both for the, interaction with the replication machinery and for the helicase activity., Functional analyses of RepA variants with single amino acid exchanges, ... [(full description)]

About this Structure

1OLO is a [Single protein] structure of sequence from [Escherichia coli] with SO4 as [ligand]. Full crystallographic information is available from [OCA].

Reference

Hexameric RSF1010 helicase RepA: the structural and functional importance of single amino acid residues., Ziegelin G, Niedenzu T, Lurz R, Saenger W, Lanka E, Nucleic Acids Res. 2003 Oct 15;31(20):5917-29. PMID:14530440

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