Distinct functions of serial metal-binding domains in the Escherichia coli P1 B -ATPase CopA
P1 B -ATPases are among the most common resistance factors to metal-induced stress. Belonging to the superfamily of P-type ATPases, they are capable of exporting transition metal ions at the expense of adenosine triphosphate (ATP) hydrolysis. P1 B -ATPases share a conserved structure of three cytopl...
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Veröffentlicht in: | Molecular microbiology 2015-08, Vol.97 (3), p.423-438 |
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creator | Drees, Steffen L Beyer, Dominik F Lenders-Lomscher, Christina Lübben, Mathias |
description | P1 B -ATPases are among the most common resistance factors to metal-induced stress. Belonging to the superfamily of P-type ATPases, they are capable of exporting transition metal ions at the expense of adenosine triphosphate (ATP) hydrolysis. P1 B -ATPases share a conserved structure of three cytoplasmic domains linked by a transmembrane domain. In addition, they possess a unique class of domains located at the N-terminus. In bacteria, these domains are primarily associated with metal binding and either occur individually or as serial copies of each other. Within this study, the roles of the two adjacent metal-binding domains (MBDs) of CopA, the copper export ATPase of Escherichia coli were investigated. From biochemical and physiological data, we deciphered the protein-internal pathway of copper and demonstrate the distal N-terminal MBD to possess a function analogous to the metallochaperones of related prokaryotic copper resistance systems, that is its involvement in the copper transfer to the membrane-integral ion-binding sites of CopA. In contrast, the proximal domain MBD2 has a regulatory role by suppressing the catalytic activity of CopA in absence of copper. Furthermore, we propose a general functional divergence of tandem MBDs in P1 B -ATPases, which is governed by the length of the inter-domain linker. |
doi_str_mv | 10.1111/mmi.13038 |
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Belonging to the superfamily of P-type ATPases, they are capable of exporting transition metal ions at the expense of adenosine triphosphate (ATP) hydrolysis. P1 B -ATPases share a conserved structure of three cytoplasmic domains linked by a transmembrane domain. In addition, they possess a unique class of domains located at the N-terminus. In bacteria, these domains are primarily associated with metal binding and either occur individually or as serial copies of each other. Within this study, the roles of the two adjacent metal-binding domains (MBDs) of CopA, the copper export ATPase of Escherichia coli were investigated. From biochemical and physiological data, we deciphered the protein-internal pathway of copper and demonstrate the distal N-terminal MBD to possess a function analogous to the metallochaperones of related prokaryotic copper resistance systems, that is its involvement in the copper transfer to the membrane-integral ion-binding sites of CopA. In contrast, the proximal domain MBD2 has a regulatory role by suppressing the catalytic activity of CopA in absence of copper. Furthermore, we propose a general functional divergence of tandem MBDs in P1 B -ATPases, which is governed by the length of the inter-domain linker.</description><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1111/mmi.13038</identifier><identifier>PMID: 25899340</identifier><language>eng</language><publisher>England</publisher><subject>Adenosine Triphosphatases - metabolism ; Binding Sites ; Cation Transport Proteins - metabolism ; Copper - metabolism ; Copper-transporting ATPases ; Escherichia coli - metabolism ; Escherichia coli Proteins ; Models, Biological ; Models, Molecular ; Protein Structure, Tertiary</subject><ispartof>Molecular microbiology, 2015-08, Vol.97 (3), p.423-438</ispartof><rights>2015 John Wiley & Sons Ltd.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25899340$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Drees, Steffen L</creatorcontrib><creatorcontrib>Beyer, Dominik F</creatorcontrib><creatorcontrib>Lenders-Lomscher, Christina</creatorcontrib><creatorcontrib>Lübben, Mathias</creatorcontrib><title>Distinct functions of serial metal-binding domains in the Escherichia coli P1 B -ATPase CopA</title><title>Molecular microbiology</title><addtitle>Mol Microbiol</addtitle><description>P1 B -ATPases are among the most common resistance factors to metal-induced stress. Belonging to the superfamily of P-type ATPases, they are capable of exporting transition metal ions at the expense of adenosine triphosphate (ATP) hydrolysis. P1 B -ATPases share a conserved structure of three cytoplasmic domains linked by a transmembrane domain. In addition, they possess a unique class of domains located at the N-terminus. In bacteria, these domains are primarily associated with metal binding and either occur individually or as serial copies of each other. Within this study, the roles of the two adjacent metal-binding domains (MBDs) of CopA, the copper export ATPase of Escherichia coli were investigated. From biochemical and physiological data, we deciphered the protein-internal pathway of copper and demonstrate the distal N-terminal MBD to possess a function analogous to the metallochaperones of related prokaryotic copper resistance systems, that is its involvement in the copper transfer to the membrane-integral ion-binding sites of CopA. In contrast, the proximal domain MBD2 has a regulatory role by suppressing the catalytic activity of CopA in absence of copper. 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Belonging to the superfamily of P-type ATPases, they are capable of exporting transition metal ions at the expense of adenosine triphosphate (ATP) hydrolysis. P1 B -ATPases share a conserved structure of three cytoplasmic domains linked by a transmembrane domain. In addition, they possess a unique class of domains located at the N-terminus. In bacteria, these domains are primarily associated with metal binding and either occur individually or as serial copies of each other. Within this study, the roles of the two adjacent metal-binding domains (MBDs) of CopA, the copper export ATPase of Escherichia coli were investigated. From biochemical and physiological data, we deciphered the protein-internal pathway of copper and demonstrate the distal N-terminal MBD to possess a function analogous to the metallochaperones of related prokaryotic copper resistance systems, that is its involvement in the copper transfer to the membrane-integral ion-binding sites of CopA. 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subjects | Adenosine Triphosphatases - metabolism Binding Sites Cation Transport Proteins - metabolism Copper - metabolism Copper-transporting ATPases Escherichia coli - metabolism Escherichia coli Proteins Models, Biological Models, Molecular Protein Structure, Tertiary |
title | Distinct functions of serial metal-binding domains in the Escherichia coli P1 B -ATPase CopA |
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