Occurrence of protein disulfide bonds in different domains of life: a comparison of proteins from the Protein Data Bank
Disulfide bonds (SS bonds) are important post-translational modifications of proteins. They stabilize a three-dimensional (3D) structure (structural SS bonds) and also have the catalytic or regulatory functions (redox-active SS bonds). Although SS bonds are present in all groups of organisms, no com...
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| Veröffentlicht in: | Protein engineering, design and selection design and selection, 2014-03, Vol.27 (3), p.65-72 |
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| container_title | Protein engineering, design and selection |
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| creator | Bošnjak, I. Bojović, V. Šegvić-Bubić, T. Bielen, A. |
| description | Disulfide bonds (SS bonds) are important post-translational modifications of proteins. They stabilize a three-dimensional (3D) structure (structural SS bonds) and also have the catalytic or regulatory functions (redox-active SS bonds). Although SS bonds are present in all groups of organisms, no comparative analyses of their frequency in proteins from different domains of life have been made to date. Using the Protein Data Bank, the number and subcellular locations of SS bonds in Archaea, Bacteria and Eukarya have been compared. Approximately three times higher frequency of proteins with SS bonds in eukaryotic secretory organelles (e.g. endoplasmic reticulum) than in bacterial periplasmic/secretory pathways was calculated. Protein length also affects the SS bond frequency: the average number of SS bonds is positively correlated with the length for longer proteins (>200 amino acids), while for the shorter and less stable proteins ( |
| doi_str_mv | 10.1093/protein/gzt063 |
| format | Article |
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Medium-sized proteins (250–350 amino acids) indicated a high number of SS bonds only in Archaea which could be explained by the need for additional protein stabilization in hyperthermophiles. The results emphasize higher capacity for the SS bond formation and isomerization in Eukarya when compared with Archaea and Bacteria.</description><identifier>ISSN: 1741-0126</identifier><identifier>EISSN: 1741-0134</identifier><identifier>DOI: 10.1093/protein/gzt063</identifier><identifier>PMID: 24407015</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Amino Acid Sequence ; Animals ; Archaea ; Bacteria ; Databases, Protein ; Disulfides - chemistry ; Intracellular Space - chemistry ; Proteins - chemistry ; Proteins - genetics</subject><ispartof>Protein engineering, design and selection, 2014-03, Vol.27 (3), p.65-72</ispartof><rights>The Author 2014. Published by Oxford University Press. All rights reserved. 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Medium-sized proteins (250–350 amino acids) indicated a high number of SS bonds only in Archaea which could be explained by the need for additional protein stabilization in hyperthermophiles. The results emphasize higher capacity for the SS bond formation and isomerization in Eukarya when compared with Archaea and Bacteria.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Archaea</subject><subject>Bacteria</subject><subject>Databases, Protein</subject><subject>Disulfides - chemistry</subject><subject>Intracellular Space - chemistry</subject><subject>Proteins - chemistry</subject><subject>Proteins - genetics</subject><issn>1741-0126</issn><issn>1741-0134</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1PwzAMhiMEYmNw5YhyhMO2uE3TjRuMT2nSOMC58hIHCm0zklYIfj0dKxM3Trasx4_sl7FjECMQ03i88q6mvBo_f9VCxTusD6mEoYBY7m77SPXYQQivQkQqBdhnvUhKkQpI-uxjoXXjPVWauLO803GTh6awuSG-dJUJ_GdkLbVgzY0rMa_Cmi9yS-ccuXblCn0eXPXHErj1ruT1C_GHznuFNfJLrN4O2Z7FItBRVwfs6eb6cXY3nC9u72cX86GWcVIPQaU4QWPISAQRQ4wTpQCtTqyMVIKYTEFEpn1FJWSJhIUlWpBaCkSNGA_Y6cbb3vTeUKizMg-aigIrck3IQE6nICfpRLXoaINq70LwZLOVz0v0nxmIbB121v2VbcJuF046d7MsyWzx33Rb4GwDuGb1n-wbSUSNwg</recordid><startdate>20140301</startdate><enddate>20140301</enddate><creator>Bošnjak, I.</creator><creator>Bojović, V.</creator><creator>Šegvić-Bubić, T.</creator><creator>Bielen, A.</creator><general>Oxford University Press</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20140301</creationdate><title>Occurrence of protein disulfide bonds in different domains of life: a comparison of proteins from the Protein Data Bank</title><author>Bošnjak, I. ; Bojović, V. ; Šegvić-Bubić, T. ; Bielen, A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c435t-167a8added4a10313a8661afc5f4265aa59102d01565efee0f1baf14c40aacaa3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Archaea</topic><topic>Bacteria</topic><topic>Databases, Protein</topic><topic>Disulfides - chemistry</topic><topic>Intracellular Space - chemistry</topic><topic>Proteins - chemistry</topic><topic>Proteins - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bošnjak, I.</creatorcontrib><creatorcontrib>Bojović, V.</creatorcontrib><creatorcontrib>Šegvić-Bubić, T.</creatorcontrib><creatorcontrib>Bielen, A.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Protein engineering, design and selection</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bošnjak, I.</au><au>Bojović, V.</au><au>Šegvić-Bubić, T.</au><au>Bielen, A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Occurrence of protein disulfide bonds in different domains of life: a comparison of proteins from the Protein Data Bank</atitle><jtitle>Protein engineering, design and selection</jtitle><addtitle>Protein Eng Des Sel</addtitle><date>2014-03-01</date><risdate>2014</risdate><volume>27</volume><issue>3</issue><spage>65</spage><epage>72</epage><pages>65-72</pages><issn>1741-0126</issn><eissn>1741-0134</eissn><abstract>Disulfide bonds (SS bonds) are important post-translational modifications of proteins. 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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Oxford University Press Journals All Titles (1996-Current); Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Archaea Bacteria Databases, Protein Disulfides - chemistry Intracellular Space - chemistry Proteins - chemistry Proteins - genetics |
| title | Occurrence of protein disulfide bonds in different domains of life: a comparison of proteins from the Protein Data Bank |
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