Tiandi Wei
Shandong University
12 Papers
42 Citations
Tiandi Wei is an academic researcher from Shandong University. The author has contributed to research in topics: Vibrio cholerae & Vibriobactin. The author has an hindex of 8, co-authored 12 publications. Previous affiliations of Tiandi Wei include Tsinghua University.
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Papers
Crystal structure of DszC from Rhodococcus sp. XP at 1.79 Å.
Shiheng Liu,Conggang Zhang,Tiantian Su,Tiandi Wei,Deyu Zhu,Kang Wang,Yan Huang,Yuhui Dong,Kun Yin,Sujuan Xu,Ping Xu,Ping Xu,Lichuan Gu +12 more
TL;DR: Site‐directed mutagenesis study shows that mutations in the residues involved either in catalysis or in flavin or substrate‐binding result in a complete loss of enzyme activity, suggesting that the accurate positions of flavin and substrate are crucial for the enzyme activity.
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Crystal structure of HutZ, a heme storage protein from Vibrio cholerae: A structural mismatch observed in the region of high sequence conservation.
Xiuhua Liu,Xiuhua Liu,Jing Gong,Tiandi Wei,Zhi Wang,Qian Du,Deyu Zhu,Yan Huang,Sujuan Xu,Lichuan Gu +9 more
TL;DR: The first crystal structure of HutZ in a homodimer determined at 2.0 Å resolution is reported and it is suggested that HutZ’s deficiency in heme oxygenase activity might derive from its residue shift relative to the heMe oxygenase HugZ.
Crystal structure of periplasmic catecholate-siderophore binding protein VctP from Vibrio cholerae at 1.7 Å resolution.
Xiuhua Liu,Qian Du,Zhi Wang,Shiheng Liu,Ning Li,Ying Chen,Chun-Yuan Zhu,Chun-Yuan Zhu,Deyu Zhu,Tiandi Wei,Yan Huang,Sujuan Xu,Lichuan Gu +12 more
TL;DR: A structural comparison of VctP with its homologues and the results of molecular docking indicate that enterobactin and vibriobactIn share the same binding pocket.
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Crystal structure of PnpCD, a two-subunit hydroquinone 1,2-dioxygenase, reveals a novel structural class of Fe2+-dependent dioxygenases
Shiheng Liu,Tiantian Su,Cong Zhang,Wen-Mao Zhang,Deyu Zhu,Jing Su,Tiandi Wei,Kang Wang,Yan Huang,Liming Guo,Sujuan Xu,Ning-Yi Zhou,Lichuan Gu +12 more
TL;DR: PnpCD reveals a new class of Fe2+-dependent dioxygenases and defines a new structural class, which contains a pseudo “cupin” and a novel iron metallocenter in the catalytic PnpD, which adds to understanding of the ring cleavage mechanism of dioXYgenases.
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Engineered Thermoplasma acidophilum factor F3 mimics human aminopeptidase N (APN) as a target for anticancer drug development.
Jing Su,Qiang Wang,Qiang Wang,Jinhong Feng,Cong Zhang,Deyu Zhu,Tiandi Wei,Wenfang Xu,Lichuan Gu +8 more
TL;DR: It is proposed here now that engineered factor F3 can be employed as a reasonable alternative of hAPN for drug design and development and discloses that compound D24 targetting the structure of E. coli APN cannot bind to the activity cleft offactor F3 with high affinity.
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