4nye | pdb_00004nye

Structures of SAICAR Synthetase (PurC) from Streptococcus pneumoniae with ADP, Mg2+, AIR and L-Asp

spinqualitylabelsall models 4nye, resolution 2.69Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4nye is a 2 chain structure with sequence from Strpn. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, ADP, CL, MG Related: 4fgr, 4fe2 Gene: purC, SP_0044 (STRPN) Activity: Phosphoribosylaminoimidazolesuccinocarboxamide synthase, with EC number 6.3.2.6 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Streptococcus pneumoniae is a multidrug-resistant pathogen that is a target of considerable interest for antibacterial drug development. One strategy for drug discovery is to inhibit an essential metabolic enzyme. The seventh step of the de novo purine-biosynthesis pathway converts carboxyaminoimidazoleribonucleotide (CAIR) and L-aspartic acid (Asp) to 4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide (SAICAR) in the presence of adenosine 5'-triphosphate (ATP) using the enzyme PurC. PurC has been shown to be conditionally essential for bacterial replication. Two crystal structures of this essential enzyme from Streptococcus pneumoniae (spPurC) in the presence of adenosine 5'-diphosphate (ADP), Mg(2+), aminoimidazoleribonucleotide (AIR) and/or Asp have been obtained. This is the first structural study of spPurC, as well as the first of PurC from any species with Asp in the active site. Based on these findings, two model structures are proposed for the active site with all of the essential ligands (ATP, Mg(2+), Asp and CAIR) present, and a relay mechanism for the formation of the product SAICAR is suggested. Structures of SAICAR synthetase (PurC) from Streptococcus pneumoniae with ADP, Mg(2+), AIR and Asp.,Wolf NM, Abad-Zapatero C, Johnson ME, Fung LW Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):841-50. doi:, 10.1107/S139900471303366X. Epub 2014 Feb 22. PMID:24598753 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA