Structural analyses reveal two distinct families of nucleoside phosphorylases.
Structural studies of the nucleoside phosphorylases have resulted in a wealth of information that begins to address fundamental biological questions, such as how Nature makes use of the intricate relationships between structure and function, and how biological processes have evolved over time.
Structure of human adenosine kinase at 1.5 A resolution.
The active-site model suggests that Asp300 is an important catalytic residue involved in the deprotonation of the 5'-hydroxyl during the phosphate transfer and represents the first structure of a new family of carbohydrate kinases.
The structural and biochemical foundations of thiamin biosynthesis.
Two thiamin degrading enzymes have been characterized and one of which is linked to a novel salvage pathway that can be salvaged through several routes, and the thiazole and pyrimidine moieties are synthesized in separate branches of the pathway.
Thiamin biosynthesis in prokaryotes
The X-ray structures of thiamin phosphate synthase and 5-hydroxyethyl-4-methylthiazole kinase have been completed and the genes coding for the thienin transport system (thiBPQ) have been identified.
Saccharomyces cerevisiae THI4p is a suicidal thiamin thiazole synthase
The preparation of fully active recombinant wild-type THI4p is reported, the identification of an iron-dependent sulphide transfer reaction from a conserved cysteine residue of the protein to a reaction intermediate and the demonstration that THI 4p is a suicide enzyme undergoing only a single turnover are reported.
Structural biology of the purine biosynthetic pathway
X-ray crystal structures are available for all 15 purine biosynthetic enzymes, including 7 ATP- dependent enzymes, 2 amidotransferases and 2 tetrahydrofolate-dependent enzymes, which discuss similarities and differences, and present arguments for pathway evolution.
Crystal structures of Toxoplasma gondii adenosine kinase reveal a novel catalytic mechanism and prodrug binding.
The 1.84 A resolution structure of an AK:7-iodotubercidin:AMP-PCP complex reveals the basis for the higher affinity binding of this prodrug over adenosine and thus provides a scaffold for the design of new inhibitors and subversive substrates that target the T. gondii AK.
Three-dimensional structure of recombinant human interferon-gamma.
The x-ray crystal structure of recombinant human interferon-gamma has been determined with the use of multiple-isomorphous-replacement techniques and is stabilized by the intertwining of helices across the subunit interface with multiple intersubunit interactions.
Flavogenomics – a genomic and structural view of flavin‐dependent proteins
A study of 374 flavin‐dependent proteins analyzed with regard to their function, structure and distribution among 22 archaeal, eubacterial, protozoan and eukaryotic genomes appears that some species depend heavily on flavIn‐dependent oxidoreductases for degradation or biosynthesis, whereas others have minimized their flavoprotein arsenal.
Calf spleen purine nucleoside phosphorylase complexed with substrates and substrate analogues.
The bovine PNP structure reveals several new details of substrate and inhibitor binding, including two phosphate-induced conformational changes involving residues 33-36 and 56-69 and a previously undetected role for His64 in phosphate binding.