Jian Hu

ORCID: 0000-0001-6657-9826
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About
Contact & Profiles
Research Areas
  • Enzyme Structure and Function
  • Trace Elements in Health
  • Amino Acid Enzymes and Metabolism
  • Protein Structure and Dynamics
  • Metal-Catalyzed Oxygenation Mechanisms
  • Metalloenzymes and iron-sulfur proteins
  • Biochemical and Molecular Research
  • Porphyrin Metabolism and Disorders
  • Microbial metabolism and enzyme function
  • Drug Transport and Resistance Mechanisms
  • Heavy Metal Exposure and Toxicity
  • Cellular transport and secretion
  • Biochemical Acid Research Studies
  • Metabolism and Genetic Disorders
  • Genetic and phenotypic traits in livestock
  • Electrochemical Analysis and Applications
  • Cancer-related molecular mechanisms research
  • Nanoparticles: synthesis and applications
  • Ginseng Biological Effects and Applications
  • Cancer, Hypoxia, and Metabolism
  • RNA modifications and cancer
  • Plant Micronutrient Interactions and Effects
  • Radioactive element chemistry and processing
  • Iron Metabolism and Disorders
  • Corrosion Behavior and Inhibition

Michigan State University
2016-2025

The University of Texas MD Anderson Cancer Center
2025

First Affiliated Hospital of Xi'an Jiaotong University
2025

Peking University People's Hospital
2017-2024

Peking University
2017-2024

Second Affiliated Hospital of Nanjing Medical University
2024

Nanjing Medical University
2016-2024

Huaian First People’s Hospital
2016-2024

Beijing University of Technology
2004-2024

Xuzhou Medical College
2024

Structures of a ZIP zinc transporter reveal an inward-open conformation with binuclear metal center in the transport pathway.

10.1126/sciadv.1700344 article EN cc-by-nc Science Advances 2017-08-04

Lactic acid racemization is involved in lactate metabolism and cell wall assembly of many microorganisms. Lactate racemase (Lar) requires nickel, but the nickel-binding site role three accessory proteins required for its activation remain enigmatic. We combined mass spectrometry x-ray crystallography to show that Lar from Lactobacillus plantarum possesses an organometallic nickel-containing prosthetic group. A nicotinic mononucleotide derivative tethered Lys(184) forms a tridentate pincer...

10.1126/science.aab2272 article EN Science 2015-07-03

The ZIP zinc transporter family is responsible for uptake from the extracellular milieu or intracellular vesicles. LIV-1 subfamily, containing nine out of 14 human proteins, featured with a large domain (ECD). critical role ECD manifested by disease-causing mutations on ZIP4, representative protein. Here we report first crystal structure mammalian ZIP4-ECD, which reveals two structurally independent subdomains and an unprecedented dimer centred at signature PAL motif. Structure-guided...

10.1038/ncomms11979 article EN cc-by Nature Communications 2016-06-20

The ethylene-forming enzyme (EFE) from Pseudomonas syringae pv. phaseolicola PK2 is a member of the mononuclear nonheme Fe(II)- and 2-oxoglutarate (2OG)-dependent oxygenase superfamily. EFE converts 2OG into ethylene plus three CO2 molecules while also catalyzing C5 hydroxylation l-arginine (l-Arg) driven by oxidative decarboxylation to form succinate CO2. Here we report 11 X-ray crystal structures that provide insight mechanisms these two reactions. Binding in absence l-Arg resulted...

10.1021/jacs.7b06186 article EN Journal of the American Chemical Society 2017-08-05

The ethylene-forming enzyme (EFE) is a non-heme Fe(II), 2-oxoglutarate (2OG), and l-arginine (l-Arg)-dependent oxygenase that catalyzes dual reactions: the generation of ethylene from 2OG C5 hydroxylation l-Arg. Using an integrated molecular dynamics (MD) quantum mechanics/molecular mechanics (QM/MM) approach references previous experimental studies, we tested hypothesis synergy between conformation l-Arg coordination mode directs reaction toward formation or hydroxylation....

10.1021/acscatal.0c03349 article EN ACS Catalysis 2021-01-19

Abstract The Zrt-/Irt-like protein (ZIP) family consists of ubiquitously expressed divalent metal transporters critically involved in maintaining systemic and cellular homeostasis zinc, iron, manganese. Here, we present a study on prokaryotic ZIP from Bordetella bronchiseptica (BbZIP) by combining structural biology, evolutionary covariance, computational modeling, variety biochemical assays to tackle the issue transport mechanism which has not been established for family. apo state...

10.1038/s41467-023-36048-4 article EN cc-by Nature Communications 2023-01-24

Andrographis paniculata (Burm. f.) Nees (APN), a principal constituent of famous traditional Chinese medicine Fukeqianjin tablet which is used for the treatment pelvic inflammatory disease (PID), has been reported to have anti-inflammatory effect in vitro. However, whether it pharmacological on PID vivo unclear. Therefore, aim this study test APN and illuminate potential mechanism. Thirty-six female specific pathogen-free SD rats were randomly divided into control group, APN1 APN2 APN3 group...

10.1186/s12906-016-1466-5 article EN cc-by BMC Complementary and Alternative Medicine 2016-11-25

Abstract Type I phosphatidylinositol phosphate kinase (PIP5K1) phosphorylates the head group of 4-phosphate (PtdIns4P) to generate PtdIns4,5P 2 , which plays important roles in a wide range cellular functions including Wnt signalling. However, lack its structural information has hindered understanding regulation. Here we report crystal structure catalytic domain zebrafish PIP5K1A at 3.3 Å resolution. This molecule forms side-to-side dimer. Mutagenesis study reveals two adjacent interfaces...

10.1038/ncomms9205 article EN cc-by Nature Communications 2015-09-14

Metal clusters are exploited by numerous metalloenzymes for catalysis, but it is not common to utilize a metal cluster substrate transport across membrane. The recent crystal structure of prototypic Zrt-/Irt-like protein (ZIP) transporter from Bordetella bronchiseptica (BbZIP) revealed an unprecedented binuclear center (BMC) within the pathway. Here, through combination bioinformatics, biochemical and structural approaches, we concluded that two physically associated metal-binding sites in...

10.1096/fj.201902043r article EN The FASEB Journal 2019-11-21

The non-heme Fe(II) and 2-oxoglutarate (2OG) dependent ethylene-forming enzyme (EFE) catalyzes both ethylene generation L-Arg hydroxylation. Despite experimental computational progress in understanding the mechanism of EFE, no EFE variant has been optimized for production while simultaneously reducing hydroxylation activity. In this study, we show that two binding conformations, associated with different reactivity preferences lead to differences intrinsic electric field (IntEF) EFE....

10.1039/d3cp01899g article EN Physical Chemistry Chemical Physics 2023-01-01

Abstract Panax ginseng is an important medicinal plant, and ginsenosides are the main bioactive molecules of ginseng. The TCP (TBI, CYC, PCF) family a group transcription factors (TFs) that play role in plant growth development, hormone signalling synthesis secondary metabolites. In our study, 78 PgTCP transcripts were identified from established transcriptome database. A phylogenetic tree analysis showed 67 with complete open reading frames classified into three subfamilies, including CIN,...

10.1186/s12870-024-04729-x article EN cc-by BMC Plant Biology 2024-01-13

The ethylene-forming enzyme (EFE) is an Fe(II), 2-oxoglutarate (2OG), and l-arginine (l-Arg)-dependent oxygenase that either forms ethylene three CO2/bicarbonate from 2OG or couples the decarboxylation of to C5 hydroxylation l-Arg. l-Arg binds with toward metal center, causing change monodentate chelate interaction OD1 OD2 switch D191 coordination. We applied anaerobic UV–visible spectroscopy, X-ray crystallography, computational approaches EFE systems high-resolution structures. ineffective...

10.1021/acs.biochem.4c00031 article EN cc-by Biochemistry 2024-04-05

Significance Thiolation reactions are essential steps in the synthesis of numerous biological metabolites. To make novel sulfur-containing cofactor LarA, an Ni-dependent lactic acid racemase, LarE catalyzes a critical sulfur transfer reaction to nicotinic acid-derived substrate by converting protein's cysteine residue dehydroalanine. In this study, crystal structures ligand-free and several ligand-bound forms provide structural basis for catalytic mechanism that is further supported...

10.1073/pnas.1704967114 article EN Proceedings of the National Academy of Sciences 2017-08-07

Bacterial lactate racemase is a nickel-dependent enzyme that contains cofactor, nickel pyridinium-3,5-bisthiocarboxylic acid mononucleotide, hereafter named nickel-pincer nucleotide (NPN). The LarC from the bacterium Lactobacillus plantarum participates in NPN biosynthesis by inserting ion into mononucleotide. This reaction, known organometallic chemistry as cyclometalation, characterized formation of new metal-carbon and metal-sulfur σ bonds. therefore first cyclometallase identified...

10.1074/jbc.ra118.003741 article EN cc-by Journal of Biological Chemistry 2018-06-10

Nutrient transporters can be rapidly removed from the cell surface via substrate-stimulated endocytosis as a way to control nutrient influx, but molecular underpinnings are not well understood. In this work, we focus on zinc-dependent of human ZIP4 (hZIP4), zinc transporter that is essential for dietary uptake. Structure-guided mutagenesis and internalization assay reveal hZIP4 per se acts exclusive sensor, with transport site's being responsible sensing. an effort seeking sorting signal,...

10.1016/j.celrep.2020.107582 article EN cc-by-nc-nd Cell Reports 2020-04-01

Magnesium ions are highly enriched in early stage of biological mineralization hard tissues. Paradoxically, hydroxyapatite (HAp) crystallization is inhibited significantly by high concentration magnesium ions. The mechanism to regulate magnesium-doped biomimetic collagen fibrils has never been fully elucidated. Herein, it revealed that citrate can bioinspire the magnesium-stabilized mineral precursors generate as follows: Citrate enhance electronegativity its absorption via hydrogen bonds....

10.1002/adhm.202303870 article EN Advanced Healthcare Materials 2024-02-27
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