5B3Q

Nqo5 of the trypsin-resistant fragment (1-134) in P63 form

Summary for 5B3Q

Entry DOI	10.2210/pdb5b3q/pdb
Related	5B3P
Descriptor	NADH-quinone oxidoreductase subunit 5 (1 entity in total)
Functional Keywords	nadh-ubiquinone oxidoreductase, complex i, oxidoreductase
Biological source	Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Total number of polymer chains	1
Total formula weight	15646.77
Authors	Hanazono, Y.,Takeda, K.,Miki, K. (deposition date: 2016-03-09, release date: 2016-07-27, Last modification date: 2023-11-08)
Primary citation	Hanazono, Y.,Takeda, K.,Miki, K. Characterization of the Nqo5 subunit of bacterial complex I in the isolated state Febs Open Bio, 6:687-695, 2016 Cited by PubMed Abstract: The subunits that comprise bacterial complex I (NADH:ubiquinone oxidoreductase) are also found in more complicated mitochondrial enzymes in eukaryotic organisms. Although the Nqo5 subunit is one of these conserved components and important for the formation of complex, it has been little studied. Here, we report structure analyses of isolated Nqo5 from Thermus thermophilus. Biochemical studies indicated that the C-terminal region following the 30-Kd subunit motif is disordered in the isolated state, while the remaining portion is already folded. Crystallographic studies of a trypsin-resistant fragment revealed detailed structural differences in the folded domain between the isolated and complexed states. PubMed: 27398308 DOI: 10.1002/2211-5463.12070 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (3.003 Å)

Structure validation