Hayden Baer

College of Agriculture and Life Sciences

2021 journal article

Structure, Function, and Thermal Adaptation of the Biotin Carboxylase Domain Dimer from Hydrogenobacter thermophilus 2-Oxoglutarate Carboxylase

BIOCHEMISTRY, 60(4), 324–345.

By: G. Buhrman n, P. Enriquez n, L. Dillard n, H. Baer n, V. Truong n, A. Grunden n, R. Rose n

MeSH headings : Bacteria / enzymology; Bacterial Proteins / chemistry; Carbon-Nitrogen Ligases / chemistry; Crystallography, X-Ray; Enzyme Stability; Hot Temperature; Protein Domains; Structure-Activity Relationship
TL;DR: Structural data reveal that the OGC BC dimer comprises a "wet" dimerization interface that is dominated by hydrophilic interactions and structural water molecules common to all BC domains and likely facilitates the conformational changes associated with the catalytic cycle. (via Semantic Scholar)
UN Sustainable Development Goal Categories
6. Clean Water and Sanitation (OpenAlex)
Sources: Web Of Science, ORCID, NC State University Libraries
Added: January 20, 2021

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