2RIF

CBS domain protein PAE2072 from Pyrobaculum aerophilum complexed with AMP

2RIF の概要

• エントリーDOI: 10.2210/pdb2rif/pdb
• 関連するPDBエントリー: 2RIH
• 分子名称: Conserved protein with 2 CBS domains, CESIUM ION, ADENOSINE MONOPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: cbs domain, bateman domain, amp binding protein, transferase, ligand-binding protein
• 由来する生物種: Pyrobaculum aerophilum
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 65483.17

構造登録者

Lee, T.M.,King, N.P.,Sawaya, M.R.,Cascio, D.,Yeates, T.O. (登録日: 2007-10-10, 公開日: 2008-06-17, 最終更新日: 2024-11-20)

主引用文献

King, N.P.,Lee, T.M.,Sawaya, M.R.,Cascio, D.,Yeates, T.O.
Structures and Functional Implications of an AMP-Binding Cystathionine beta-Synthase Domain Protein from a Hyperthermophilic Archaeon.
J.Mol.Biol., 380:181-192, 2008

PubMed Abstract: Cystathionine beta-synthase domains are found in a myriad of proteins from organisms across the tree of life and have been hypothesized to function as regulatory modules that sense the energy charge of cells. Here we characterize the structure and stability of PAE2072, a dimeric tandem cystathionine beta-synthase domain protein from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum. Crystal structures of the protein in unliganded and AMP-bound forms, determined at resolutions of 2.10 and 2.35 A, respectively, reveal remarkable conservation of key functional features seen in the gamma subunit of the eukaryotic AMP-activated protein kinase. The structures also confirm the presence of a suspected intermolecular disulfide bond between the two subunits that is shown to stabilize the protein. Our AMP-bound structure represents a first step in investigating the function of a large class of uncharacterized prokaryotic proteins. In addition, this work extends previous studies that have suggested that, in certain thermophilic microbes, disulfide bonds play a key role in stabilizing intracellular proteins and protein-protein complexes.

PubMed: 18513746
DOI: 10.1016/j.jmb.2008.04.073

実験手法

X-RAY DIFFRACTION (2.35 Å)