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5TCE

N-terminal microdomain of 34-mers from HsDHODH - N-t(DH)

Summary for 5TCE
Entry DOI10.2210/pdb5tce/pdb
NMR InformationBMRB: 30180
DescriptorDihydroorotate dehydrogenase (quinone), mitochondrial (1 entity in total)
Functional Keywordsmicelles, oxidoreductase
Biological sourceHomo sapiens (Human)
Total number of polymer chains1
Total formula weight3831.32
Authors
Crusca, E.,Munte, C.E. (deposition date: 2016-09-14, release date: 2017-09-20, Last modification date: 2024-10-16)
Primary citationVicente, E.F.,Sahu, I.D.,Costa-Filho, A.J.,Cilli, E.M.,Lorigan, G.A.
Conformational changes of the HsDHODH N-terminal Microdomain via DEER Spectroscopy.
J Phys Chem B, 119:8693-8697, 2015
Cited by
PubMed Abstract: The human enzyme dihydroorotate dehydrogenase (HsDHODH) has been studied for being a target for development of new antineoplasic and antiproliferative drugs. The synthetic peptide N-t(DH) represents the N-terminal microdomain of this enzyme, responsible for anchoring it to the inner mitochondrial membrane. Also, it is known to harbor quinones that are essential for enzyme catalysis. Here we report structural features of the peptide/membrane interactions obtained by using CD and DEER spectroscopic techniques, both in micelles and in lipid vesicles. The data revealed different peptide conformational states in micelles and liposomes, which could suggest that this microdomain acts in specific regions or areas of the mitochondria, which can be related with the control of the quinone access to the HsDHODH active site. This is the first study to report on conformational changes of the HsDHODH N-terminal microdomain through a combination of CD and DEER spectroscopic techniques.
PubMed: 26086954
DOI: 10.1021/acs.jpcb.5b01706
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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