NMR assignment of human ubiquitin conjugating enzyme Ubc7
NMR assignment of human ubiquitin conjugating enzyme Ubc7
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DOI:
10.1007/s10858-005-1257-7
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发表时间:
2005-08-01
影响因子:
2.7
通讯作者:
Tolman, JR
中科院分区:
文献类型:
--
作者:
Briggman, KB;Majumdar, A;Tolman, JR
The malaria parasite Plasmodium falciparum spends part of its life cycle in human erythrocytes, where it is challenged with enhanced oxidative stress, and where it needs efficient anti-oxidants to maintain its reducing milieu and to protect itself against damage (Rahlfs et al., 2002). Thioredoxin (PfTrx) is one of the major redoxregulatory molecules which, because of its dithiol/disulfide exchange activity, determines the oxidation state of protein cysteines, being therefore a potential target in research towards anti-malarial drugs (Kanzok et al., 2000). We initiated the structure determination of the recombinant 104-amino acid polypeptide, using multidimensional NMR spectroscopy. Sequential backbone resonance assignments were carried out on the basis of HNCA, CBCA (CO) NH, CBCANH, HNCO, 1H) 15N-HSQC and 1H) 15N-NOESY-HSQC experiments. Side-chain assignments were done using the HCCH-TOCSY experiment with the sample in 2H2O. The chemical shifts for 99% of the backbone1HN, 13Ca 15NH (without considering the proline residues), for 89% of the 13C′, 99% of the 1Ha, and 88% of all side-chain atoms (except the 13C shifts of the aromatic rings) of the PfTrx were assigned. Data were deposited in the BioMagResBank under accession number 6442. References: Kanzok et al.(2000) J. Biol. Chem., 275, 40181–40186; Rahlfs et al.(2002) Cell. Mol. Life Sci., 59, 1024–1041.