1g19

From Proteopedia

proteopedia linkproteopedia link

spinqualitylabelsall models 1g19, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURE OF RECA PROTEIN

Overview

Sequencing of the complete genome of Mycobacterium tuberculosis, combined, with the rapidly increasing need to improve tuberculosis management, through better drugs and vaccines, has initiated extensive research on, several key proteins from the pathogen. RecA, a ubiquitous multifunctional, protein, is a key component of the processes of homologous genetic, recombination and DNA repair. Structural knowledge of MtRecA is imperative, for a full understanding of both these activities and any ensuing, application. The crystal structure of MtRecA, presented here, has six, molecules in the unit cell forming a 6(1) helical filament with a deep, groove capable of binding DNA. The observed weakening in the higher order, aggregation of filaments into bundles may have implications for, recombination in mycobacteria. The structure of the complex reveals the, atomic interactions of ADP-AlF(4), an ATP analogue, with the, P-loop-containing binding pocket. The structures explain reduced levels of, interactions of MtRecA with ATP, despite sharing the same fold, topology, and high sequence similarity with EcRecA. The formation of a helical, filament with a deep groove appears to be an inherent property of MtRecA., The histidine in loop L1 appears to be positioned appropriately for DNA, interaction.

About this Structure

1G19 is a Single protein structure of sequence from Mycobacterium tuberculosis with PO4 as ligand. Active as Deleted entry, with EC number 3.4.99.37 Full crystallographic information is available from OCA.

Reference

Crystal structures of Mycobacterium tuberculosis RecA and its complex with ADP-AlF(4): implications for decreased ATPase activity and molecular aggregation., Datta S, Prabu MM, Vaze MB, Ganesh N, Chandra NR, Muniyappa K, Vijayan M, Nucleic Acids Res. 2000 Dec 15;28(24):4964-73. PMID:11121488

Page seeded by OCA on Tue Nov 20 15:36:59 2007