2nv2 | pdb_00002nv2

Structure of the PLP synthase complex Pdx1/2 (YaaD/E) from Bacillus subtilis

spinqualitylabelsall models 2nv2, resolution 2.12Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2nv2 is a 24 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, EDO, GLN Related: 1znn, 1r9g, 2nv0, 2nv1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PDXS_BACSU] Involved in the production of pyridoxal phosphate, probably by incorporating ammonia into the pyridine ring.[HAMAP-Rule:MF_01824] [PDXT_BACSU] Involved in the hydrolysis of glutamine to glutamate and ammonia. Channels an ammonia molecule to PdxS. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Vitamin B6 is an essential metabolic cofactor that has more functions in humans than any other single nutrient. Its de novo biosynthesis occurs through two mutually exclusive pathways that are absent in animals. The predominant pathway found in most prokaryotes, fungi, and plants has only recently been discovered. It is distinguished by a glutamine amidotransferase, which is remarkable in that it alone can synthesize the cofactor form, pyridoxal 5'-phosphate (PLP), directly from a triose and a pentose saccharide and glutamine. Here we report the 3D structure of the PLP synthase complex with substrate glutamine bound as well as those of the individual synthase and glutaminase subunits Pdx1 and Pdx2, respectively. The complex is made up of 24 protein units assembled like a cogwheel, a dodecameric Pdx1 to which 12 Pdx2 subunits attach. In contrast to the architecture of previously determined glutamine amidotransferases, macromolecular assembly is directed by an N-terminal alpha-helix on the synthase. Interaction with the synthase subunit leads to glutaminase activation, resulting in formation of an oxyanion hole, a prerequisite for catalysis. Mutagenesis permitted identification of the remote glutaminase and synthase catalytic centers and led us to propose a mechanism whereby ammonia shuttles between these active sites through a methionine-rich hydrophobic tunnel. Structure of a bacterial pyridoxal 5'-phosphate synthase complex.,Strohmeier M, Raschle T, Mazurkiewicz J, Rippe K, Sinning I, Fitzpatrick TB, Tews I Proc Natl Acad Sci U S A. 2006 Dec 19;103(51):19284-9. Epub 2006 Dec 11. PMID:17159152 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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