1VEI

Mycobacterium smegmatis Dps

1VEI の概要

• エントリーDOI: 10.2210/pdb1vei/pdb
• 関連するPDBエントリー: 1VEL 1VEQ
• 分子名称: starvation-induced DNA protecting protein, FE (III) ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: dna-binding protein, dna binding protein
• 由来する生物種: Mycobacterium smegmatis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20506.56

構造登録者

Roy, S.,Gupta, S.,Das, S.,Sekar, K.,Chatterji, D.,Vijayan, M. (登録日: 2004-03-31, 公開日: 2004-06-29, 最終更新日: 2023-12-27)

主引用文献

Roy, S.,Gupta, S.,Das, S.,Sekar, K.,Chatterji, D.,Vijayan, M.
X-ray Analysis of Mycobacterium smegmatis Dps and a Comparative Study Involving Other Dps and Dps-like Molecules
J.Mol.Biol., 339:1103-1113, 2004

PubMed Abstract: The structure of the DNA binding protein from starved cells from Mycobacterium smegmatis has been determined in three crystal forms and has been compared with those of similar proteins from other sources. The dodecameric molecule can be described as a distorted icosahedron. The interfaces among subunits are such that the dodecameric molecule appears to have been made up of stable trimers. The situation is similar in the proteins from Escherichia coli and Agrobacterium tumefaciens, which are closer to the M.smegmatis protein in sequence and structure than those from other sources, which appear to form a dimer first. Trimerisation is aided in the three proteins by the additional N-terminal stretches that they possess. The M.smegmatis protein has an additional C-terminal stretch compared to other related proteins. The stretch, known to be involved in DNA binding, is situated on the surface of the molecule. A comparison of the available structures permits a delineation of the rigid and flexible regions in the molecule. The subunit interfaces around the molecular dyads, where the ferroxidation centres are located, are relatively rigid. Regions in the vicinity of the acidic holes centred around molecular 3-fold axes, are relatively flexible. So are the DNA binding regions. The crystal structures of the protein from M.smegmatis confirm that DNA molecules can occupy spaces within the crystal without disturbing the arrangement of the protein molecules. However, contrary to earlier suggestions, the spaces do not need to be between layers of protein molecules. The cubic form provides an arrangement in which grooves, which could hold DNA molecules, criss-cross the crystal.

PubMed: 15178251
DOI: 10.1016/j.jmb.2004.04.042

実験手法

X-RAY DIFFRACTION (2.85 Å)