Electron paramagnetic resonance characterization of the copper-resistance protein PcoC from Escherichia coli
Continuous-wave and pulsed electron paramagnetic resonance have been applied to the study of the Cu II site of the copper-resistance protein PcoC from Escherichia coli and certain variant forms. Electron spin echo envelope modulation (ESEEM) experiments confirm the presence of two histidine ligands,...
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Veröffentlicht in: | Journal of biological inorganic chemistry 2008-08, Vol.13 (6), p.899-907 |
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container_title | Journal of biological inorganic chemistry |
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creator | Drew, Simon C. Djoko, Karrera Y. Zhang, Lianyi Koay, Melissa Boas, John F. Pilbrow, John R. Xiao, Zhiguang Barnham, Kevin J. Wedd, Anthony G. |
description | Continuous-wave and pulsed electron paramagnetic resonance have been applied to the study of the Cu
II
site of the copper-resistance protein PcoC from
Escherichia coli
and certain variant forms. Electron spin echo envelope modulation (ESEEM) experiments confirm the presence of two histidine ligands, His1 and His92, at the Cu
II
site of wild-type PcoC, consistent with the available X-ray crystallographic data for the homolog CopC (67% sequence identity) from
Pseudomonas syringae
pv.
tomato
. The variants H1F and H92F each lack one of the histidine residues close to the Cu
II
site. The ESEEM data suggest that the surviving histidine residue remains as a ligand. The nA variant features an extra alanine residue at the N terminus, which demotes the His1 ligand to position 2. At least one of the two histidine residues is bound at the Cu
II
site in this form. Simulation of the
14
N superhyperfine structure in the continuous-wave spectra confirms the presence of at least three nitrogen-based ligands at the Cu
II
sites of the wild-type, H92F and nA forms, while the H1F variant has two nitrogen ligands. The spectra of wild-type form can be fitted adequately with a 3N or a 4N model. The former is consistent with the crystal structure of the CopC homolog, where His1 acts as a bidentate ligand. The latter raises the possibility of an additional unidentified nitrogen ligand. The markedly different spectra of the H1F and nA forms compared with the wild-type and H92F proteins further highlight the integral role of the N-terminal histidine residue in the high-affinity Cu
II
site of PcoC. |
doi_str_mv | 10.1007/s00775-008-0377-4 |
format | Article |
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II
site of the copper-resistance protein PcoC from
Escherichia coli
and certain variant forms. Electron spin echo envelope modulation (ESEEM) experiments confirm the presence of two histidine ligands, His1 and His92, at the Cu
II
site of wild-type PcoC, consistent with the available X-ray crystallographic data for the homolog CopC (67% sequence identity) from
Pseudomonas syringae
pv.
tomato
. The variants H1F and H92F each lack one of the histidine residues close to the Cu
II
site. The ESEEM data suggest that the surviving histidine residue remains as a ligand. The nA variant features an extra alanine residue at the N terminus, which demotes the His1 ligand to position 2. At least one of the two histidine residues is bound at the Cu
II
site in this form. Simulation of the
14
N superhyperfine structure in the continuous-wave spectra confirms the presence of at least three nitrogen-based ligands at the Cu
II
sites of the wild-type, H92F and nA forms, while the H1F variant has two nitrogen ligands. The spectra of wild-type form can be fitted adequately with a 3N or a 4N model. The former is consistent with the crystal structure of the CopC homolog, where His1 acts as a bidentate ligand. The latter raises the possibility of an additional unidentified nitrogen ligand. The markedly different spectra of the H1F and nA forms compared with the wild-type and H92F proteins further highlight the integral role of the N-terminal histidine residue in the high-affinity Cu
II
site of PcoC.</description><identifier>ISSN: 0949-8257</identifier><identifier>EISSN: 1432-1327</identifier><identifier>DOI: 10.1007/s00775-008-0377-4</identifier><identifier>PMID: 18421485</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer-Verlag</publisher><subject>Binding Sites ; Biochemistry ; Biomedical and Life Sciences ; Crystallography, X-Ray ; Electron Spin Resonance Spectroscopy ; Escherichia coli - chemistry ; Escherichia coli Proteins - chemistry ; Life Sciences ; Ligands ; Microbiology ; Models, Molecular ; Molecular Structure ; Original Paper ; Sensitivity and Specificity</subject><ispartof>Journal of biological inorganic chemistry, 2008-08, Vol.13 (6), p.899-907</ispartof><rights>SBIC 2008</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c342t-40f704a58e248be2b3c8400bfcb87d9e46386ce41d017c96a331b06917c6ac8b3</citedby><cites>FETCH-LOGICAL-c342t-40f704a58e248be2b3c8400bfcb87d9e46386ce41d017c96a331b06917c6ac8b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00775-008-0377-4$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00775-008-0377-4$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18421485$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Drew, Simon C.</creatorcontrib><creatorcontrib>Djoko, Karrera Y.</creatorcontrib><creatorcontrib>Zhang, Lianyi</creatorcontrib><creatorcontrib>Koay, Melissa</creatorcontrib><creatorcontrib>Boas, John F.</creatorcontrib><creatorcontrib>Pilbrow, John R.</creatorcontrib><creatorcontrib>Xiao, Zhiguang</creatorcontrib><creatorcontrib>Barnham, Kevin J.</creatorcontrib><creatorcontrib>Wedd, Anthony G.</creatorcontrib><title>Electron paramagnetic resonance characterization of the copper-resistance protein PcoC from Escherichia coli</title><title>Journal of biological inorganic chemistry</title><addtitle>J Biol Inorg Chem</addtitle><addtitle>J Biol Inorg Chem</addtitle><description>Continuous-wave and pulsed electron paramagnetic resonance have been applied to the study of the Cu
II
site of the copper-resistance protein PcoC from
Escherichia coli
and certain variant forms. Electron spin echo envelope modulation (ESEEM) experiments confirm the presence of two histidine ligands, His1 and His92, at the Cu
II
site of wild-type PcoC, consistent with the available X-ray crystallographic data for the homolog CopC (67% sequence identity) from
Pseudomonas syringae
pv.
tomato
. The variants H1F and H92F each lack one of the histidine residues close to the Cu
II
site. The ESEEM data suggest that the surviving histidine residue remains as a ligand. The nA variant features an extra alanine residue at the N terminus, which demotes the His1 ligand to position 2. At least one of the two histidine residues is bound at the Cu
II
site in this form. Simulation of the
14
N superhyperfine structure in the continuous-wave spectra confirms the presence of at least three nitrogen-based ligands at the Cu
II
sites of the wild-type, H92F and nA forms, while the H1F variant has two nitrogen ligands. The spectra of wild-type form can be fitted adequately with a 3N or a 4N model. The former is consistent with the crystal structure of the CopC homolog, where His1 acts as a bidentate ligand. The latter raises the possibility of an additional unidentified nitrogen ligand. The markedly different spectra of the H1F and nA forms compared with the wild-type and H92F proteins further highlight the integral role of the N-terminal histidine residue in the high-affinity Cu
II
site of PcoC.</description><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Crystallography, X-Ray</subject><subject>Electron Spin Resonance Spectroscopy</subject><subject>Escherichia coli - chemistry</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Life Sciences</subject><subject>Ligands</subject><subject>Microbiology</subject><subject>Models, Molecular</subject><subject>Molecular Structure</subject><subject>Original Paper</subject><subject>Sensitivity and Specificity</subject><issn>0949-8257</issn><issn>1432-1327</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1PxCAURYnR6PjxA9yYrtyhj0ILXZrJ-JFMogtdE8q8Opi2VGAW-utlnEncuYHwOPcGDiGXDG4YgLyNeZEVBVAUuJRUHJAZE7ykjJfykMygEQ1VZSVPyGmMHwDAK1YdkxOmRMmEqmakX_RoU_BjMZlgBvM-YnK2CBj9aEaLhV3nuU0Y3LdJLnO-K9I6z_00YaAZdDH9klPwCd1YvFg_L7rgh2IR7ToH7dqZzPfunBx1po94sd_PyNv94nX-SJfPD0_zuyW1XJSJCugkCFMpLIVqsWy5VQKg7Wyr5KpBUXNVWxRsBUzapjacsxbqJh9qY1XLz8j1rjc_6XODMenBRYt9b0b0m6jrhleiBpFBtgNt8DEG7PQU3GDCl2agt4r1TrHOivVWsd5mrvblm3bA1V9i7zQD5Q6I-Wp8x6A__CaM-cP_tP4Aq9KIdA</recordid><startdate>20080801</startdate><enddate>20080801</enddate><creator>Drew, Simon C.</creator><creator>Djoko, Karrera Y.</creator><creator>Zhang, Lianyi</creator><creator>Koay, Melissa</creator><creator>Boas, John F.</creator><creator>Pilbrow, John R.</creator><creator>Xiao, Zhiguang</creator><creator>Barnham, Kevin J.</creator><creator>Wedd, Anthony G.</creator><general>Springer-Verlag</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>20080801</creationdate><title>Electron paramagnetic resonance characterization of the copper-resistance protein PcoC from Escherichia coli</title><author>Drew, Simon C. ; Djoko, Karrera Y. ; Zhang, Lianyi ; Koay, Melissa ; Boas, John F. ; Pilbrow, John R. ; Xiao, Zhiguang ; Barnham, Kevin J. ; Wedd, Anthony G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c342t-40f704a58e248be2b3c8400bfcb87d9e46386ce41d017c96a331b06917c6ac8b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Binding Sites</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Crystallography, X-Ray</topic><topic>Electron Spin Resonance Spectroscopy</topic><topic>Escherichia coli - chemistry</topic><topic>Escherichia coli Proteins - chemistry</topic><topic>Life Sciences</topic><topic>Ligands</topic><topic>Microbiology</topic><topic>Models, Molecular</topic><topic>Molecular Structure</topic><topic>Original Paper</topic><topic>Sensitivity and Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Drew, Simon C.</creatorcontrib><creatorcontrib>Djoko, Karrera Y.</creatorcontrib><creatorcontrib>Zhang, Lianyi</creatorcontrib><creatorcontrib>Koay, Melissa</creatorcontrib><creatorcontrib>Boas, John F.</creatorcontrib><creatorcontrib>Pilbrow, John R.</creatorcontrib><creatorcontrib>Xiao, Zhiguang</creatorcontrib><creatorcontrib>Barnham, Kevin J.</creatorcontrib><creatorcontrib>Wedd, Anthony G.</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>Journal of biological inorganic chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Drew, Simon C.</au><au>Djoko, Karrera Y.</au><au>Zhang, Lianyi</au><au>Koay, Melissa</au><au>Boas, John F.</au><au>Pilbrow, John R.</au><au>Xiao, Zhiguang</au><au>Barnham, Kevin J.</au><au>Wedd, Anthony G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Electron paramagnetic resonance characterization of the copper-resistance protein PcoC from Escherichia coli</atitle><jtitle>Journal of biological inorganic chemistry</jtitle><stitle>J Biol Inorg Chem</stitle><addtitle>J Biol Inorg Chem</addtitle><date>2008-08-01</date><risdate>2008</risdate><volume>13</volume><issue>6</issue><spage>899</spage><epage>907</epage><pages>899-907</pages><issn>0949-8257</issn><eissn>1432-1327</eissn><abstract>Continuous-wave and pulsed electron paramagnetic resonance have been applied to the study of the Cu
II
site of the copper-resistance protein PcoC from
Escherichia coli
and certain variant forms. Electron spin echo envelope modulation (ESEEM) experiments confirm the presence of two histidine ligands, His1 and His92, at the Cu
II
site of wild-type PcoC, consistent with the available X-ray crystallographic data for the homolog CopC (67% sequence identity) from
Pseudomonas syringae
pv.
tomato
. The variants H1F and H92F each lack one of the histidine residues close to the Cu
II
site. The ESEEM data suggest that the surviving histidine residue remains as a ligand. The nA variant features an extra alanine residue at the N terminus, which demotes the His1 ligand to position 2. At least one of the two histidine residues is bound at the Cu
II
site in this form. Simulation of the
14
N superhyperfine structure in the continuous-wave spectra confirms the presence of at least three nitrogen-based ligands at the Cu
II
sites of the wild-type, H92F and nA forms, while the H1F variant has two nitrogen ligands. The spectra of wild-type form can be fitted adequately with a 3N or a 4N model. The former is consistent with the crystal structure of the CopC homolog, where His1 acts as a bidentate ligand. The latter raises the possibility of an additional unidentified nitrogen ligand. The markedly different spectra of the H1F and nA forms compared with the wild-type and H92F proteins further highlight the integral role of the N-terminal histidine residue in the high-affinity Cu
II
site of PcoC.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer-Verlag</pub><pmid>18421485</pmid><doi>10.1007/s00775-008-0377-4</doi><tpages>9</tpages></addata></record> |
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subjects | Binding Sites Biochemistry Biomedical and Life Sciences Crystallography, X-Ray Electron Spin Resonance Spectroscopy Escherichia coli - chemistry Escherichia coli Proteins - chemistry Life Sciences Ligands Microbiology Models, Molecular Molecular Structure Original Paper Sensitivity and Specificity |
title | Electron paramagnetic resonance characterization of the copper-resistance protein PcoC from Escherichia coli |
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