1FX7

CRYSTAL STRUCTURE OF THE IRON-DEPENDENT REGULATOR (IDER) FROM MYCOBACTERIUM TUBERCULOSIS

1FX7 の概要

• エントリーDOI: 10.2210/pdb1fx7/pdb
• 関連するPDBエントリー: 1b1b 1bi0 1bi1 1bi2 1bi3 1bym 1c0w 1ddn 1dpr 2dtr 2tdx
• 分子名称: IRON-DEPENDENT REPRESSOR IDER, SULFATE ION, COBALT (II) ION, ... (4 entities in total)
• 機能のキーワード: ider, dtxr, iron-dependent regulator, mycobacterium tuberculosis, signaling protein
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 103526.58

構造登録者

Feese, M.D.,Ingason, B.P.,Goranson-Siekierke, J.,Holmes, R.K.,Hol, W.J.G. (登録日: 2000-09-25, 公開日: 2001-03-07, 最終更新日: 2024-02-07)

主引用文献

Feese, M.D.,Ingason, B.P.,Goranson-Siekierke, J.,Holmes, R.K.,Hol, W.G.
Crystal structure of the iron-dependent regulator from Mycobacterium tuberculosis at 2.0-A resolution reveals the Src homology domain 3-like fold and metal binding function of the third domain.
J.Biol.Chem., 276:5959-5966, 2001

PubMed Abstract: Iron-dependent regulators are primary transcriptional regulators of virulence factors and iron scavenging systems that are important for infection by several bacterial pathogens. Here we present the 2.0-A crystal structure of the wild type iron-dependent regulator from Mycobacterium tuberculosis in its fully active holorepressor conformation. Clear, unbiased electron density for the Src homology domain 3-like third domain, which is often invisible in structures of iron-dependent regulators, was revealed by density modification and averaging. This domain is one of the rare examples of Src homology domain 3-like folds in bacterial proteins, and, in addition, displays a metal binding function by contributing two ligands, one Glu and one Gln, to the pentacoordinated cobalt atom at metal site 1. Both metal sites are fully occupied, and tightly bound water molecules at metal site 1 ("Water 1") and metal site 2 ("Water 2") are identified unambiguously. The main chain carbonyl of Leu4 makes an indirect interaction with the cobalt atom at metal site 2 via Water 2, and the adjacent residue, Val5, forms a rare gamma turn. Residues 1-3 are well ordered and make numerous interactions. These ordered solvent molecules and the conformation and interactions of the N-terminal pentapeptide thus might be important in metal-dependent activation.

PubMed: 11053439
DOI: 10.1074/jbc.M007531200

実験手法

X-RAY DIFFRACTION (2 Å)