ArticleBiochemistry2006
Structural insights into the mechanism of the PLP synthase holoenzyme from Thermotoga maritima.
Article in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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29 citing papers in PubMed, 80 citations in OpenAlex.
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- Structure and dynamics of the staphylococcal pyridoxal 5-phosphate synthase complex reveal transient interactions at the enzyme interface.The Journal of biological chemistry · 2024Article
- Trapping and structural characterisation of a covalent intermediate in vitamin BRSC chemical biology · 2022Article
- Structural Characterization of Multienzyme Assemblies: An Overview.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Recombinant Expression, Purification and Characterization of Pyridoxal 5'-phosphate Synthase fromIranian journal of biotechnology · 2021Article
- Structural Dynamics and Perspectives of Vitamin B6 Biosynthesis Enzymes inFrontiers in cellular and infection microbiology · 2021Review
- Solution Structures and Dynamic Assembly of the 24-Meric Plasmodial Pdx1-Pdx2 Complex.International journal of molecular sciences · 2020Article
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- First insights of peptidoglycan amidation in Gram-positive bacteria - the high-resolution crystal structure of Staphylococcus aureus glutamine amidotransferase GatD.Scientific reports · 2018Article
- Lysine relay mechanism coordinates intermediate transfer in vitamin B6 biosynthesis.Nature chemical biology · 2017Article
- Structural definition of the lysine swing in Arabidopsis thaliana PDX1: Intermediate channeling facilitating vitamin B6 biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Crystal structures capture three states in the catalytic cycle of a pyridoxal phosphate (PLP) synthase.The Journal of biological chemistry · 2015Article
- Consequences of a deficit in vitamin B6 biosynthesis de novo for hormone homeostasis and root development in Arabidopsis.Plant physiology · 2015Article
- The pseudoenzyme PDX1.2 boosts vitamin B6 biosynthesis under heat and oxidative stress in Arabidopsis.The Journal of biological chemistry · 2014Article
- Crystal structure of pyridoxal biosynthesis lyase PdxS from Pyrococcus horikoshii.Molecules and cells · 2012Article
- Overexpression, crystallization and preliminary X-ray crystallographic analysis of pyridoxal biosynthesis lyase PdxS from Pyrococcus horikoshii.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Identification and in vitro analysis of the GatD/MurT enzyme-complex catalyzing lipid II amidation in Staphylococcus aureus.PLoS pathogens · 2012Article
- It takes two to tango: defining an essential second active site in pyridoxal 5'-phosphate synthase.PloS one · 2011Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Pyridoxal 5'-phosphate (PLP) is the biologically active form of vitamin B6 and is an important cofactor for several of the enzymes involved in the metabolism of amine-containing natural products such as amino acids and amino sugars. The PLP synthase holoenzyme consists of two subunits: YaaD catalyzes the condensation of ribulose 5-phosphate, glyceraldehyde-3-phosphate, and ammonia, and YaaE catalyzes the production of ammonia from glutamine. Here we describe the structure of the PLP synthase complex (YaaD-YaaE) from Thermotoga maritima at 2.9 A resolution. This complex consists of a core of 12 YaaD monomers with 12 noninteracting YaaE monomers attached to the core. Compared with the previously published structure of PdxS (a YaaD ortholog in Geobacillus stearothermophilus), the N-terminus (1-18), which includes helix alpha0, the beta2-alpha2 loop (46-56), which includes new helix alpha2a, and the C-terminus (270-280) of YaaD are ordered in the complex but disordered in PdxS. A ribulose 5-phosphate is bound to YaaD via an imine with Lys82. Previous studies have demonstrated a similar imine at Lys149 and not at Lys81 (equivalent to Lys150 and Lys82 in T. maritima) for the Bacillus subtilis enzyme suggesting the possibility that two separate sites on YaaD are involved in PLP formation. A phosphate from the crystallization solution is found bound to YaaD and also serves as a marker for a possible second active site. An ammonia channel that connects the active site of YaaE with the ribulose 5-phosphate binding site was identified. This channel is similar to one found in imidazole glycerol phosphate synthase; however, when the beta-barrels of the two complexes are superimposed, the glutaminase domains are rotated by about 180 degrees with respect to each other.
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