1ue5

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Revision as of 01:56, 21 November 2007

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spinqualitylabelsall models 1ue5, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of the single-stranded dna-binding protein from mycobacterium tuberculosis

Overview

Single-stranded DNA-binding protein (SSB) is an essential protein, necessary for the functioning of the DNA replication, repair and, recombination machineries. Here we report the structure of the DNA-binding, domain of Mycobacterium tuberculosis SSB (MtuSSB) in four different, crystals distributed in two forms. The structure of one of the forms was, solved by a combination of isomorphous replacement and anomalous, scattering. This structure was used to determine the structure of the, other form by molecular replacement. The polypeptide chain in the, structure exhibits the oligonucleotide binding fold. The globular core of, the molecule in different subunits in the two forms and those in, Escherichia coli SSB (EcoSSB) and human mitochondrial SSB (HMtSSB) have, similar structure, although the three loops exhibit considerable, structural variation. However, the tetrameric MtuSSB has an as yet, unobserved quaternary association. This quaternary structure with a unique, dimeric interface lends the oligomeric protein greater stability, which, may be of significance to the functioning of the protein under conditions, of stress. Also, as a result of the variation in the quaternary structure, the path adopted by the DNA to wrap around MtuSSB is expected to be, different from that of EcoSSB.

About this Structure

1UE5 is a Single protein structure of sequence from Mycobacterium tuberculosis with CD as ligand. Full crystallographic information is available from OCA.

Reference

Structure of Mycobacterium tuberculosis single-stranded DNA-binding protein. Variability in quaternary structure and its implications., Saikrishnan K, Jeyakanthan J, Venkatesh J, Acharya N, Sekar K, Varshney U, Vijayan M, J Mol Biol. 2003 Aug 8;331(2):385-93. PMID:12888346

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