2RIF
CBS domain protein PAE2072 from Pyrobaculum aerophilum complexed with AMP
Summary for 2RIF
| Entry DOI | 10.2210/pdb2rif/pdb |
| Related | 2RIH |
| Descriptor | Conserved protein with 2 CBS domains, CESIUM ION, ADENOSINE MONOPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | cbs domain, bateman domain, amp binding protein, transferase, ligand-binding protein |
| Biological source | Pyrobaculum aerophilum |
| Total number of polymer chains | 4 |
| Total formula weight | 65483.17 |
| Authors | Lee, T.M.,King, N.P.,Sawaya, M.R.,Cascio, D.,Yeates, T.O. (deposition date: 2007-10-10, release date: 2008-06-17, Last modification date: 2017-10-25) |
| Primary citation | 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 Cited by 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: 18513746DOI: 10.1016/j.jmb.2008.04.073 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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