The structural principles underlying molybdenum insertase complex assembly

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F23%3A00131582" target="_blank" >RIV/00216224:14740/23:00131582 - isvavai.cz</a>

Result on the web

<a href="https://onlinelibrary.wiley.com/doi/full/10.1002/pro.4753" target="_blank" >https://onlinelibrary.wiley.com/doi/full/10.1002/pro.4753</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/pro.4753" target="_blank" >10.1002/pro.4753</a>

Result language

angličtina

Original language name

The structural principles underlying molybdenum insertase complex assembly

Original language description

Within the cell, the trace element molybdenum (Mo) is only biologically active when complexed either within the nitrogenase-specific FeMo cofactor or within the molybdenum cofactor (Moco). Moco consists of an organic part, called molybdopterin (MPT) and an inorganic part, that is, the Mo-center. The enzyme which catalyzes the Mo-center formation is the molybdenum insertase (Mo-insertase). Mo-insertases consist of two functional domains called G- and E-domain. The G-domain catalyzes the formation of adenylated MPT (MPT-AMP), which is the substrate for the E-domain, that catalyzes the actual molybdate insertion reaction. Though the functions of E- and G-domain have been elucidated to great structural and mechanistic detail, their combined function is poorly characterized. In this work, we describe a structural model of the eukaryotic Mo-insertase Cnx1 complex that was generated based on cross-linking mass spectrometry combined with computational modeling. We revealed Cnx1 to form an asymmetric hexameric complex which allows the E- and G-domain active sites to align in a catalytic productive orientation toward each other.

Czech name

—

Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10608 - Biochemistry and molecular biology

Project

—

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2023

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Protein Science

ISSN

0961-8368

e-ISSN

1469-896X

Volume of the periodical

32

Issue of the periodical within the volume

9

Country of publishing house

US - UNITED STATES

Number of pages

13

Pages from-to

1-13

UT code for WoS article

001058430700004

EID of the result in the Scopus database

2-s2.0-85169470188