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The Metal-binding Protein Atlas (MbPA): An Integrated Database for Curating Metalloproteins in All Aspects

[Display omitted] •MbPA is the most comprehensive resource of metal type, binding sites, sequences, structures and proteomics of metal-binding protein across multiple species.•MbPA embraces potential pathogenic mutations related to metalloprotein.•The Diversity Measure is firstly employed to describ...

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Published in:Journal of molecular biology 2023-07, Vol.435 (14), p.168117-168117, Article 168117
Main Authors: Li, Jinzhao, He, Xiang, Gao, Shuang, Liang, Yuchao, Qi, Zhi, Xi, Qilemuge, Zuo, Yongchun, Xing, Yongqiang
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cited_by cdi_FETCH-LOGICAL-c396t-15726c71595add3659ff63ed80a790cc23054464fd6772bcf0e0def61f6817103
cites cdi_FETCH-LOGICAL-c396t-15726c71595add3659ff63ed80a790cc23054464fd6772bcf0e0def61f6817103
container_end_page 168117
container_issue 14
container_start_page 168117
container_title Journal of molecular biology
container_volume 435
creator Li, Jinzhao
He, Xiang
Gao, Shuang
Liang, Yuchao
Qi, Zhi
Xi, Qilemuge
Zuo, Yongchun
Xing, Yongqiang
description [Display omitted] •MbPA is the most comprehensive resource of metal type, binding sites, sequences, structures and proteomics of metal-binding protein across multiple species.•MbPA embraces potential pathogenic mutations related to metalloprotein.•The Diversity Measure is firstly employed to describe the specificity of metal-binding in different area of periodic table. 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.
doi_str_mv 10.1016/j.jmb.2023.168117
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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. 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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. 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subjects Amino Acids - chemistry
Binding Sites
Cations - chemistry
diversity measure
metal-binding proteins
Metalloproteins - chemistry
Metalloproteins - genetics
Metals - chemistry
mutation information
protein structures
title The Metal-binding Protein Atlas (MbPA): An Integrated Database for Curating Metalloproteins in All Aspects
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