Active site rearrangement and structural divergence in prokaryotic respiratory oxidases
Cytochrome bd–type quinol oxidases catalyze the reduction of molecular oxygen to water in the respiratory chain of many human-pathogenic bacteria. They are structurally unrelated to mitochondrial cytochrome c oxidases and are therefore a prime target for the development of antimicrobial drugs. We de...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2019-10, Vol.366 (6461), p.100-104 |
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| creator | Safarian, S. Hahn, A. Mills, D. J. Radloff, M. Eisinger, M. L. Nikolaev, A. Meier-Credo, J. Melin, F. Miyoshi, H. Gennis, R. B. Sakamoto, J. Langer, J. D. Hellwig, P. Kühlbrandt, W. Michel, H. |
| description | Cytochrome bd–type quinol oxidases catalyze the reduction of molecular oxygen to water in the respiratory chain of many human-pathogenic bacteria. They are structurally unrelated to mitochondrial cytochrome c oxidases and are therefore a prime target for the development of antimicrobial drugs. We determined the structure of the Escherichia coli cytochrome bd-I oxidase by single-particle cryo–electron microscopy to a resolution of 2.7 angstroms. Our structure contains a previously unknown accessory subunit CydH, the L-subfamily–specific Q-loop domain, a structural ubiquinone-8 cofactor, an active-site density interpreted as dioxygen, distinct water-filled proton channels, and an oxygen-conducting pathway. Comparison with another cytochrome bd oxidase reveals structural divergence in the family, including rearrangement of high-spin hemes and conformational adaption of a transmembrane helix to generate a distinct oxygen-binding site. |
| doi_str_mv | 10.1126/science.aay0967 |
| format | Article |
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J. ; Radloff, M. ; Eisinger, M. L. ; Nikolaev, A. ; Meier-Credo, J. ; Melin, F. ; Miyoshi, H. ; Gennis, R. B. ; Sakamoto, J. ; Langer, J. D. ; Hellwig, P. ; Kühlbrandt, W. ; Michel, H.</creator><creatorcontrib>Safarian, S. ; Hahn, A. ; Mills, D. J. ; Radloff, M. ; Eisinger, M. L. ; Nikolaev, A. ; Meier-Credo, J. ; Melin, F. ; Miyoshi, H. ; Gennis, R. B. ; Sakamoto, J. ; Langer, J. D. ; Hellwig, P. ; Kühlbrandt, W. ; Michel, H.</creatorcontrib><description>Cytochrome bd–type quinol oxidases catalyze the reduction of molecular oxygen to water in the respiratory chain of many human-pathogenic bacteria. They are structurally unrelated to mitochondrial cytochrome c oxidases and are therefore a prime target for the development of antimicrobial drugs. We determined the structure of the Escherichia coli cytochrome bd-I oxidase by single-particle cryo–electron microscopy to a resolution of 2.7 angstroms. Our structure contains a previously unknown accessory subunit CydH, the L-subfamily–specific Q-loop domain, a structural ubiquinone-8 cofactor, an active-site density interpreted as dioxygen, distinct water-filled proton channels, and an oxygen-conducting pathway. Comparison with another cytochrome bd oxidase reveals structural divergence in the family, including rearrangement of high-spin hemes and conformational adaption of a transmembrane helix to generate a distinct oxygen-binding site.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.aay0967</identifier><identifier>PMID: 31604309</identifier><language>eng</language><publisher>United States: American Association for the Advancement of Science</publisher><subject>Antiinfectives and antibacterials ; Antimicrobial agents ; Bacteria ; Binding sites ; Biochemistry, Molecular Biology ; Catalytic Domain ; Channels ; Coenzyme Q8 ; Cofactors ; Coliforms ; Cryoelectron Microscopy ; Cytochrome ; Cytochrome b Group - chemistry ; Cytochrome bd ; Cytochrome c ; Cytochromes ; Divergence ; Drug development ; E coli ; Electron microscopy ; Electron transport ; Electron Transport Chain Complex Proteins - chemistry ; Enzymes ; Escherichia coli ; Escherichia coli - enzymology ; Escherichia coli Proteins - chemistry ; Heme ; Heme - chemistry ; Homology ; Hydroquinone ; Life Sciences ; Microscopy ; Mitochondria ; Models, Molecular ; Oxidase ; Oxidation-Reduction ; Oxidoreductases - chemistry ; Oxygen ; Oxygen - chemistry ; Protein Structure, Quaternary ; Protein Subunits - chemistry ; Protons ; Quinol oxidase ; Reduction ; Relocation ; Structure-function relationships ; Terminal oxidase ; Ubiquinone ; Ubiquinone - chemistry ; Water</subject><ispartof>Science (American Association for the Advancement of Science), 2019-10, Vol.366 (6461), p.100-104</ispartof><rights>Copyright © 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.</rights><rights>Copyright © 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c484t-c616b1d6e273a71ae4949e2298456fa695f9c161bc2220dc685432ec687fbcac3</citedby><cites>FETCH-LOGICAL-c484t-c616b1d6e273a71ae4949e2298456fa695f9c161bc2220dc685432ec687fbcac3</cites><orcidid>0000-0003-0904-1119 ; 0000-0003-4118-5438 ; 0000-0002-2013-4810 ; 0000-0001-6294-5163 ; 0000-0003-0934-913X ; 0000-0001-6557-7028 ; 0000-0002-1792-554X ; 0000-0003-4351-7846 ; 0000-0001-7543-1778 ; 0000-0002-5190-577X ; 0000-0003-0827-5642</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,2871,2872,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31604309$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-03341532$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Safarian, S.</creatorcontrib><creatorcontrib>Hahn, A.</creatorcontrib><creatorcontrib>Mills, D. J.</creatorcontrib><creatorcontrib>Radloff, M.</creatorcontrib><creatorcontrib>Eisinger, M. L.</creatorcontrib><creatorcontrib>Nikolaev, A.</creatorcontrib><creatorcontrib>Meier-Credo, J.</creatorcontrib><creatorcontrib>Melin, F.</creatorcontrib><creatorcontrib>Miyoshi, H.</creatorcontrib><creatorcontrib>Gennis, R. B.</creatorcontrib><creatorcontrib>Sakamoto, J.</creatorcontrib><creatorcontrib>Langer, J. D.</creatorcontrib><creatorcontrib>Hellwig, P.</creatorcontrib><creatorcontrib>Kühlbrandt, W.</creatorcontrib><creatorcontrib>Michel, H.</creatorcontrib><title>Active site rearrangement and structural divergence in prokaryotic respiratory oxidases</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>Cytochrome bd–type quinol oxidases catalyze the reduction of molecular oxygen to water in the respiratory chain of many human-pathogenic bacteria. They are structurally unrelated to mitochondrial cytochrome c oxidases and are therefore a prime target for the development of antimicrobial drugs. We determined the structure of the Escherichia coli cytochrome bd-I oxidase by single-particle cryo–electron microscopy to a resolution of 2.7 angstroms. Our structure contains a previously unknown accessory subunit CydH, the L-subfamily–specific Q-loop domain, a structural ubiquinone-8 cofactor, an active-site density interpreted as dioxygen, distinct water-filled proton channels, and an oxygen-conducting pathway. Comparison with another cytochrome bd oxidase reveals structural divergence in the family, including rearrangement of high-spin hemes and conformational adaption of a transmembrane helix to generate a distinct oxygen-binding site.</description><subject>Antiinfectives and antibacterials</subject><subject>Antimicrobial agents</subject><subject>Bacteria</subject><subject>Binding sites</subject><subject>Biochemistry, Molecular Biology</subject><subject>Catalytic Domain</subject><subject>Channels</subject><subject>Coenzyme Q8</subject><subject>Cofactors</subject><subject>Coliforms</subject><subject>Cryoelectron Microscopy</subject><subject>Cytochrome</subject><subject>Cytochrome b Group - chemistry</subject><subject>Cytochrome bd</subject><subject>Cytochrome c</subject><subject>Cytochromes</subject><subject>Divergence</subject><subject>Drug development</subject><subject>E coli</subject><subject>Electron microscopy</subject><subject>Electron transport</subject><subject>Electron Transport Chain Complex Proteins - chemistry</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Heme</subject><subject>Heme - chemistry</subject><subject>Homology</subject><subject>Hydroquinone</subject><subject>Life Sciences</subject><subject>Microscopy</subject><subject>Mitochondria</subject><subject>Models, Molecular</subject><subject>Oxidase</subject><subject>Oxidation-Reduction</subject><subject>Oxidoreductases - chemistry</subject><subject>Oxygen</subject><subject>Oxygen - chemistry</subject><subject>Protein Structure, Quaternary</subject><subject>Protein Subunits - chemistry</subject><subject>Protons</subject><subject>Quinol oxidase</subject><subject>Reduction</subject><subject>Relocation</subject><subject>Structure-function relationships</subject><subject>Terminal oxidase</subject><subject>Ubiquinone</subject><subject>Ubiquinone - chemistry</subject><subject>Water</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkUFv2zAMhYVhRZt1Pe-0wcAu68EtJcqydQyKdi0QoJcWOwqKTHfKHDuT5GL591WQLIeeCJAfyUc-xr5wuOJcqOvoPA2Orqzdglb1BzbjoKtSC8CPbAaAqmygrs7YpxhXALmm8ZSdIVcgEfSM_Zq75F-piD5REciGYIcXWtOQCju0RUxhcmkKti_ajIWX3bbCD8UmjH9s2I7Ju9wWNz7YNIZtMf7zrY0UP7OTzvaRLg7xnD3f3T7d3JeLx58PN_NF6WQjU-kUV0veKhI12ppbklpqEkI3slKdVbrqtOOKL50QAlqnmkqioBzrbumsw3N2uZ_72_ZmE_w6izKj9eZ-vjC7HCBKXqF45Zn9sWez-L8TxWTWPjrqezvQOEUjECqQGmqV0e_v0NU4hSFfsqNAKeQImbreUy6MMQbqjgo4mJ0_5uCPOfiTO74d5k7LNbVH_r8hGfi6B1Yx__NYF6qRWDWIby6ol10</recordid><startdate>20191004</startdate><enddate>20191004</enddate><creator>Safarian, S.</creator><creator>Hahn, A.</creator><creator>Mills, D. 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J.</au><au>Radloff, M.</au><au>Eisinger, M. L.</au><au>Nikolaev, A.</au><au>Meier-Credo, J.</au><au>Melin, F.</au><au>Miyoshi, H.</au><au>Gennis, R. B.</au><au>Sakamoto, J.</au><au>Langer, J. D.</au><au>Hellwig, P.</au><au>Kühlbrandt, W.</au><au>Michel, H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Active site rearrangement and structural divergence in prokaryotic respiratory oxidases</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>2019-10-04</date><risdate>2019</risdate><volume>366</volume><issue>6461</issue><spage>100</spage><epage>104</epage><pages>100-104</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><abstract>Cytochrome bd–type quinol oxidases catalyze the reduction of molecular oxygen to water in the respiratory chain of many human-pathogenic bacteria. 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| subjects | Antiinfectives and antibacterials Antimicrobial agents Bacteria Binding sites Biochemistry, Molecular Biology Catalytic Domain Channels Coenzyme Q8 Cofactors Coliforms Cryoelectron Microscopy Cytochrome Cytochrome b Group - chemistry Cytochrome bd Cytochrome c Cytochromes Divergence Drug development E coli Electron microscopy Electron transport Electron Transport Chain Complex Proteins - chemistry Enzymes Escherichia coli Escherichia coli - enzymology Escherichia coli Proteins - chemistry Heme Heme - chemistry Homology Hydroquinone Life Sciences Microscopy Mitochondria Models, Molecular Oxidase Oxidation-Reduction Oxidoreductases - chemistry Oxygen Oxygen - chemistry Protein Structure, Quaternary Protein Subunits - chemistry Protons Quinol oxidase Reduction Relocation Structure-function relationships Terminal oxidase Ubiquinone Ubiquinone - chemistry Water |
| title | Active site rearrangement and structural divergence in prokaryotic respiratory oxidases |
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