2OXG
The SoxYZ Complex of Paracoccus pantotrophus
Summary for 2OXG
Entry DOI | 10.2210/pdb2oxg/pdb |
Related | 2OX5 |
Descriptor | SoxZ protein, SoxY protein, SULFATE ION, ... (5 entities in total) |
Functional Keywords | immunoglobulin-like beta-sandwich fold, transport protein |
Biological source | Paracoccus denitrificans More |
Total number of polymer chains | 8 |
Total formula weight | 97032.76 |
Authors | Sauve, V.,Berks, B.C.,Hemmings, A.M. (deposition date: 2007-02-20, release date: 2007-05-22, Last modification date: 2023-08-30) |
Primary citation | Sauve, V.,Bruno, S.,Berks, B.C.,Hemmings, A.M. The SoxYZ Complex Carries Sulfur Cycle Intermediates on a Peptide Swinging Arm. J.Biol.Chem., 282:23194-23204, 2007 Cited by PubMed Abstract: The bacterial Sox (sulfur oxidizing) system allows the utilization of inorganic sulfur compounds in energy metabolism. Central to this process is the SoxYZ complex that carries the pathway intermediates on a cysteine residue near the C terminus of SoxY. Crystal structures have been determined for Paracoccus pantotrophus SoxYZ with the carrier cysteine in the underivatized state, conjugated to the polysulfide mimic beta-mercaptoethanol, and as the sulfonate adduct pathway intermediate. The carrier cysteine is located on a peptide swinging arm and is bracketed on either side by diglycine dipeptides acting as molecular universal joints. This structure provides a novel solution to the requirement that the cysteine-bound intermediates be able to access and orient themselves within the active sites of multiple partner enzymes. Adjacent to the swinging arm there is a conserved, deep, apolar pocket into which the beta-mercaptoethanol adduct extends. This pocket would be well suited to a role in protecting labile pathway intermediates from adventitious reactions. PubMed: 17522046DOI: 10.1074/jbc.M701602200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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