Reflect and Reset: Black Academic Voices Call the Graduate Medical Education Community to Action.

The COVID-19 pandemic highlighted the great achievements that the biomedical community can accomplish, but raised the question: Can the same medical community that developed a complex vaccine in less than a year during a pandemic help to defeat social injustice and ameliorate the epidemic of health inequity? In this article, the authors, a group of Black academics, call on the graduate medical education (GME) community to reset its trajectory toward solutions for achieving diversity, improving inclusion, and combating racism using education as the new vector. Sponsoring institutions, which include universities, academic medical centers, teaching hospitals, and teaching health centers, are the center of the creation and dissemination of scholarship. They are often the main sources of care for many historically marginalized communities. The GME learning environment must provide the next generation of medical professionals with an understanding of how racism continues to have a destructive influence on health care professionals and their patients. Residents have the practical experience of longitudinal patient care, and a significant portion of an individual's professional identity is formed during GME; therefore, this is a key time to address explicit stereotyping and to identify implicit bias at the individual level. The authors propose 3 main reset strategies for GME-incorporating inclusive pedagogy and structural competency into education, building a diverse and inclusive learning environment, and activating community engagement-as well as tactics that sponsoring institutions can adapt to address racism at the individual learner, medical education program, and institutional levels. Sustained, comprehensive, and systematic implementation of multiple tactics could make a significant impact. It is an academic and moral imperative for the medical community to contribute to the design and implementation of solutions that directly address racism, shifting how resident physicians are educated and modeling just and inclusive behaviors for the next generation of medical leaders.

Mutational and structural analyses of Caldanaerobius polysaccharolyticus Man5B reveal novel active site residues for family 5 glycoside hydrolases.

CpMan5B is a glycoside hydrolase (GH) family 5 enzyme exhibiting both ß-1,4-mannosidic and ß-1,4-glucosidic cleavage activities. To provide insight into the amino acid residues that contribute to catalysis and substrate specificity, we solved the structure of CpMan5B at 1.6 Å resolution. The structure revealed several active site residues (Y12, N92 and R196) in CpMan5B that are not present in the active sites of other structurally resolved GH5 enzymes. Residue R196 in GH5 enzymes is thought to be strictly conserved as a histidine that participates in an electron relay network with the catalytic glutamates, but we show that an arginine fulfills a functionally equivalent role and is found at this position in every enzyme in subfamily GH5_36, which includes CpMan5B. Residue N92 is required for full enzymatic activity and forms a novel bridge over the active site that is absent in other family 5 structures. Our data also reveal a role of Y12 in establishing the substrate preference for CpMan5B. Using these molecular determinants as a probe allowed us to identify Man5D from Caldicellulosiruptor bescii as a mannanase with minor endo-glucanase activity.