1UE5

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

1UE5 の概要

• エントリーDOI: 10.2210/pdb1ue5/pdb
• 関連するPDBエントリー: 1UE1 1UE6 1UE7
• 分子名称: Single-strand binding protein, CADMIUM ION (3 entities in total)
• 機能のキーワード: oligonucleotide binding fold, dna-binding protein, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, dna binding protein
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34968.95

構造登録者

Saikrishnan, K.,Jeyakanthan, J.,Venkatesh, J.,Acharya, N.,Sekar, K.,Varshney, U.,Vijayan, M.,TB Structural Genomics Consortium (TBSGC) (登録日: 2003-05-09, 公開日: 2004-02-10, 最終更新日: 2023-10-25)

主引用文献

Saikrishnan, K.,Jeyakanthan, J.,Venkatesh, J.,Acharya, N.,Sekar, K.,Varshney, U.,Vijayan, M.
Structure of Mycobacterium tuberculosis single-stranded DNA-binding protein. Variability in quaternary structure and its implications
J.MOL.BIOL., 331:385-393, 2003

PubMed Abstract: 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.

PubMed: 12888346
DOI: 10.1016/S0022-2836(03)00729-0

実験手法

X-RAY DIFFRACTION (2.6 Å)