Další formáty:
BibTeX
LaTeX
RIS
@article{2306338,
author = {Hassan, Ahmed Adel Ibrahim Hassona and Ihling, Christian and Iacobucci, Claudio and Kastritis, Panagiotis L and Sinz, Andrea and Kruse, Tobias},
article_location = {MALDEN},
article_number = {9},
doi = {http://dx.doi.org/10.1002/pro.4753},
keywords = {biosynthesis complex; molybdenum cofactor; molybdenum insertase},
language = {eng},
issn = {0961-8368},
journal = {Protein Science},
title = {The structural principles underlying molybdenum insertase complex assembly},
url = {https://onlinelibrary.wiley.com/doi/full/10.1002/pro.4753},
volume = {32},
year = {2023}
}
TY - JOUR
ID - 2306338
AU - Hassan, Ahmed Adel Ibrahim Hassona - Ihling, Christian - Iacobucci, Claudio - Kastritis, Panagiotis L - Sinz, Andrea - Kruse, Tobias
PY - 2023
TI - The structural principles underlying molybdenum insertase complex assembly
JF - Protein Science
VL - 32
IS - 9
SP - 1-13
EP - 1-13
PB - WILEY-BLACKWELL
SN - 09618368
KW - biosynthesis complex
KW - molybdenum cofactor
KW - molybdenum insertase
UR - https://onlinelibrary.wiley.com/doi/full/10.1002/pro.4753
N2 - 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.
ER -
HASSAN, Ahmed Adel Ibrahim Hassona, Christian IHLING, Claudio IACOBUCCI, Panagiotis L KASTRITIS, Andrea SINZ a Tobias KRUSE. The structural principles underlying molybdenum insertase complex assembly. \textit{Protein Science}. MALDEN: WILEY-BLACKWELL, 2023, roč.~32, č.~9, s.~1-13. ISSN~0961-8368. Dostupné z: https://dx.doi.org/10.1002/pro.4753.
|
