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Metal-binding proteins are essential for the vital activities and engage in their roles by acting in concert with metal cations. MbPA (The Metal-binding Protein Atlas) is the most comprehensive resource up to now dedicated to curating metal-binding proteins. Currently, it contains 106,373 entries and 440,187 sites related to 54 metals and 8169 species. Users can view all metal-binding proteins and species-specific proteins in MbPA. There are also metal-proteomics data that quantitatively describes protein expression in different tissues and organs. By analyzing the data of the amino acid residues at the metal-binding site, it is found that about 80% of the metal ions tend to bind to cysteine, aspartic acid, glutamic acid, and histidine. Moreover, we use Diversity Measure to confirm that the diversity of metal-binding is specific in different area of periodic table, and further elucidate the binding modes of 19 transition metals on 20 amino acids. In addition, MbPA also embraces 6855 potential pathogenic mutations related to metalloprotein. The resource is freely available at http://bioinfor.imu.edu.cn/mbpa.
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http://dx.doi.org/10.1016/j.jmb.2023.168117 | DOI Listing |
Magn Reson Lett
February 2025
State Key Laboratory of Elemento-organic Chemistry, College of Chemistry, Nankai University, Tianjin, 300071, China.
Rat sarcoma virus oncogene (RAS) proteins are of crucial oncogenic proteins and are involved in several essential intracellular processes. The RAS protein has an intrinsic metal binding site for Mg, which is important for the conformational stability of the active site. Recently, it was reported that a second metal ion binding site, located further from the active site in HRAS (Harvey RAS homolog), binds Ca with millimolar affinity.
View Article and Find Full Text PDFJ Mol Graph Model
September 2025
College of General Education, Kookmin University, Seoul, 02707, Republic of Korea. Electronic address:
Green fluorescent proteins (GFPs) are optical markers that are widely used in molecular and cell biology studies to track the location and function of biomolecules. Elucidating their structures will facilitate further engineering of these fluorescent proteins (FPs) to enhance their properties. AlphaFold3 (AF3) is a recently developed prediction tool that exhibits higher accuracy compared with other prediction tools, particularly in predicting protein-ligand interactions with state-of-the-art docking tools.
View Article and Find Full Text PDFJ Am Chem Soc
September 2025
Department of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina 29208, United States.
Iron homeostasis is essential for the virulence of the opportunistic fungal pathogen . The cytosolic monothiol glutaredoxin GrxD was recently shown to play a critical role in iron metabolism via regulation of iron-sulfur (Fe-S) binding iron-responsive transcription factors and interaction with components of the cytosolic Fe-S cluster assembly pathway. Interestingly, the putative copper-binding metallothionein CmtA was also identified as a binding partner for GrxD; however, the metal-binding properties of both proteins and the nature of their interactions were unclear.
View Article and Find Full Text PDFRSC Adv
August 2025
Department of Chemistry, University of California, Davis One Shields Avenue Davis CA 95616 USA
Imbalances in cellular copper are increasingly implicated in metabolic disorders. Food-derived peptides are gaining attention for their ability to alleviate metabolic disease symptoms with little to no toxicity. In this work, we enriched copper-binding peptides from enzymatic digestions of rice bran protein hydrolysates Cu(ii)-based immobilized-metal affinity-based separations, identified the sequences by mass spectrometry, and performed physicochemical and sequence analysis of the enriched peptides.
View Article and Find Full Text PDFCarbon and zinc (Zn) metabolism are intrinsically connected in phototrophs, as crucial components involved in CO assimilation, like carbonic anhydrases, are highly abundant Zn proteins. Utilizing these and other proteins, the eukaryotic green algae can maintain phototrophic growth in low CO environments by inducing a carbon concentrating mechanism (CCM). In this work we show that Chlamydomonas dynamically increases its Zn content to accommodate the higher intracellular Zn demand in low CO environments.
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