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Single particle cryo-EM structure of the Neisseria meningitidis quinol-dependent nitric oxide reductase (NmqNOR)


ABSTRACT:

SUBMITTER: Chai C Gopalasingam 

PROVIDER: EMPIAR-13360 | biostudies-other |

REPOSITORIES: biostudies-other

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Structural basis of Neisseria meningitidis quinol dependent nitric oxide reductase activation by dimerization.

Gopalasingam Chai C CC   Egami Haruka H   Shigematsu Hideki H   Sakaue Masatora M   Fukumoto Kouki K   Gerle Christoph C   Yamamoto Masaki M   Shiro Yoshitsugu Y   Muramoto Kazumasa K   Tosha Takehiko T  

Communications biology 20260327 1


In all kingdoms of life, the regulation of membrane-bound enzyme function via oligomerization is a fundamental aspect of cell physiology. Often, the mechanistic role of oligomerization is unclear, due to a lack of structure-function comparisons between constituent forms of the enzyme. Here, we elucidate the structural underpinnings of enzyme regulation and oligomerization in the quinol-dependent nitric oxide reductase (qNOR) from Neisseria meningitidis, by high-resolution structural analyses of  ...[more]

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