The World Health Organization reported that in 2017 almost 31,000 newborns died from exposure to tetanus neurotoxin (TeNT), which is produced by the bacterium Clostridium tetani, despite there being an effective vaccine available. When an individual is exposed to TeNT, the toxin travels through the bloodstream to the peripheral nervous system (PNS) where it is trafficked to the central nervous system (CNS). TeNT cleaves vesicle‐associated membrane protein‐2 (VAMP2), a membrane protein in the CNS, blocking the release of neurotransmitters which signal muscle cells to relax, thus resulting in spastic paralysis. TeNT has two separate domains, A and B. The A domain is a protease and the B domain contains both an N‐terminal translocation domain (HCT/T) and a C‐terminal receptor binding domain (HCR/T). HCR/T is made up of 450 residues, arranged into six alpha helices and 33 beta sheets. HCR/T has two important carbohydrate‐binding pockets. The Arg1226‐containing “R” pocket binds sialic acid on b‐series gangliosides (i.e. GT1b), while the Trp1289‐containing “W” pocket binds to sugar groups on a‐series gangliosides (i.e. GM1a). Functioning “R” and “W” pockets are essential for TeNT toxicity. The Cedarburg High School SMART (Students Modeling A Research Topic) Team has designed a model of HCR/T using 3D printing technology to investigate TeNT structure‐function relationships. Further investigation into how TeNT moves from the PNS into the CNS can help elucidate new methods to cure or prevent tetanus, especially in newborn infants in developing countries where the mortality rate is significant. Support or Funding Information National Institutes of Health Clinical and Translational Science Award (NIH‐CTSA UL1RR031973)

Infections caused by antibiotic‐resistant pathogens like MRSA are serious problems that require the development of new antibiotics. The non‐proteinogenic amino acid L‐enduracididine (L‐End) is looked at as a solution, as it could be used to synthesize new versions of L‐End‐containing antibiotics and improve drug efficacy of antibiotics not normally containing L‐End. However, L‐End is difficult to synthesize and is not commercially available. The enzyme MppP, an L‐arginine deaminase/hydroxylase from Streptomyces wadayamensis, is involved in L‐Arg biosynthesis. MppP is a pyridoxal 5′‐phosphate (PLP)‐dependent oxidase catalyzing the oxidation of L‐Arg to 2‐oxo‐4‐hydroxy‐guanidinovaleric acid, which continues along the pathway to produce L‐End. Four electrons are transferred to L‐Arg from molecular oxygen via the PLP cofactor; water contributes the hydroxyl and ketone oxygen atoms of the product. MppP functions as a homodimer. Each 376‐residue protomer contains a large domain, primarily composed of beta sheets, and a smaller domain consisting of a mix of alpha helices and beta sheets. The active site, containing PLP and the catalytic Lys221, is located between these two domains. The N‐terminal portion of the protein is not ordered unless substrate or product is bound in the active site, and this region appears to be critical for catalysis. The Cedarburg SMART (Students Modeling A Research Topic) Team has designed a model of MppP using 3D printing technology to investigate MppP structure‐function relationships. Studying the structure and function of MppP can elucidate the mechanism of L‐End biosynthesis, making possible the commercial production of L‐End for use in new MRSA‐fighting antibiotics.This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.