Crystal structure of acetoacetyl‐CoA reductase from Rickettsia felis
Rickettsia felis, a Gram‐negative bacterium that causes spotted fever, is of increasing interest as an emerging human pathogen. R. felis and several other Rickettsia strains are classed as National Institute of Allergy and Infectious Diseases priority pathogens. In recent years, R. felis has been sh...
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description | Rickettsia felis, a Gram‐negative bacterium that causes spotted fever, is of increasing interest as an emerging human pathogen. R. felis and several other Rickettsia strains are classed as National Institute of Allergy and Infectious Diseases priority pathogens. In recent years, R. felis has been shown to be adaptable to a wide range of hosts, and many fevers of unknown origin are now being attributed to this infectious agent. Here, the structure of acetoacetyl‐CoA reductase from R. felis is reported at a resolution of 2.0 Å. While R. felis acetoacetyl‐CoA reductase shares less than 50% sequence identity with its closest homologs, it adopts a fold common to other short‐chain dehydrogenase/reductase (SDR) family members, such as the fatty‐acid synthesis II enzyme FabG from the prominent pathogens Staphylococcus aureus and Bacillus anthracis. Continued characterization of the Rickettsia proteome may prove to be an effective means of finding new avenues of treatment through comparative structural studies.
The structure of acetoacetyl‐CoA reductase from Rickettsia felis, the causative agent of flea‐borne spotted fever, is reported. Acetoacetyl‐CoA reductase is a key enzyme in both the glyoxylate/dicarboxylate and butanoate metabolic pathways. |
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The structure of acetoacetyl‐CoA reductase from Rickettsia felis, the causative agent of flea‐borne spotted fever, is reported. Acetoacetyl‐CoA reductase is a key enzyme in both the glyoxylate/dicarboxylate and butanoate metabolic pathways.</description><identifier>ISSN: 2053-230X</identifier><identifier>EISSN: 2053-230X</identifier><identifier>DOI: 10.1107/S2053230X21001497</identifier><identifier>PMID: 33620038</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography</publisher><subject>acetoacetyl‐CoA reductase ; Alcohol Oxidoreductases - chemistry ; Alcohol Oxidoreductases - genetics ; Alcohol Oxidoreductases - isolation & purification ; Alcohol Oxidoreductases - metabolism ; Allergies ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - isolation & purification ; Bacterial Proteins - metabolism ; Crystal structure ; Crystallography, X-Ray ; Fever ; Homology ; Infectious diseases ; Models, Molecular ; oxidoreductase ; Pathogens ; PhaB ; Protein Conformation ; Proteomes ; Reductase ; Reductases ; Research Communications ; Rickettsia ; Rickettsia felis ; Rickettsia felis - enzymology ; Seattle Structural Genomics Center for Infectious Disease ; SSGCID ; structural genomics</subject><ispartof>Acta crystallographica. Section F, Structural biology communications, 2021-02, Vol.77 (2), p.54-60</ispartof><rights>2021 Rodarte et al. published by IUCr Journals.</rights><rights>Copyright Wiley Subscription Services, Inc. Feb 2021</rights><rights>Rodarte et al. 2021 2021</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4342-ac57c4dc31834ffde6e56d24fef99b573bd57dc1dea66c79f3bb48e3700fbc7f3</citedby><cites>FETCH-LOGICAL-c4342-ac57c4dc31834ffde6e56d24fef99b573bd57dc1dea66c79f3bb48e3700fbc7f3</cites><orcidid>0000-0002-7497-3206</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7900926/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7900926/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,1411,27901,27902,45550,45551,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33620038$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rodarte, Justas V.</creatorcontrib><creatorcontrib>Abendroth, Jan</creatorcontrib><creatorcontrib>Edwards, Thomas E.</creatorcontrib><creatorcontrib>Lorimer, Donald D.</creatorcontrib><creatorcontrib>Staker, Bart L.</creatorcontrib><creatorcontrib>Zhang, Sunny</creatorcontrib><creatorcontrib>Myler, Peter J.</creatorcontrib><creatorcontrib>McLaughlin, Krystle J.</creatorcontrib><title>Crystal structure of acetoacetyl‐CoA reductase from Rickettsia felis</title><title>Acta crystallographica. Section F, Structural biology communications</title><addtitle>Acta Crystallogr F Struct Biol Commun</addtitle><description>Rickettsia felis, a Gram‐negative bacterium that causes spotted fever, is of increasing interest as an emerging human pathogen. R. felis and several other Rickettsia strains are classed as National Institute of Allergy and Infectious Diseases priority pathogens. In recent years, R. felis has been shown to be adaptable to a wide range of hosts, and many fevers of unknown origin are now being attributed to this infectious agent. Here, the structure of acetoacetyl‐CoA reductase from R. felis is reported at a resolution of 2.0 Å. While R. felis acetoacetyl‐CoA reductase shares less than 50% sequence identity with its closest homologs, it adopts a fold common to other short‐chain dehydrogenase/reductase (SDR) family members, such as the fatty‐acid synthesis II enzyme FabG from the prominent pathogens Staphylococcus aureus and Bacillus anthracis. Continued characterization of the Rickettsia proteome may prove to be an effective means of finding new avenues of treatment through comparative structural studies.
The structure of acetoacetyl‐CoA reductase from Rickettsia felis, the causative agent of flea‐borne spotted fever, is reported. Acetoacetyl‐CoA reductase is a key enzyme in both the glyoxylate/dicarboxylate and butanoate metabolic pathways.</description><subject>acetoacetyl‐CoA reductase</subject><subject>Alcohol Oxidoreductases - chemistry</subject><subject>Alcohol Oxidoreductases - genetics</subject><subject>Alcohol Oxidoreductases - isolation & purification</subject><subject>Alcohol Oxidoreductases - metabolism</subject><subject>Allergies</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - isolation & purification</subject><subject>Bacterial Proteins - metabolism</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>Fever</subject><subject>Homology</subject><subject>Infectious diseases</subject><subject>Models, Molecular</subject><subject>oxidoreductase</subject><subject>Pathogens</subject><subject>PhaB</subject><subject>Protein Conformation</subject><subject>Proteomes</subject><subject>Reductase</subject><subject>Reductases</subject><subject>Research Communications</subject><subject>Rickettsia</subject><subject>Rickettsia felis</subject><subject>Rickettsia felis - enzymology</subject><subject>Seattle Structural Genomics Center for Infectious Disease</subject><subject>SSGCID</subject><subject>structural genomics</subject><issn>2053-230X</issn><issn>2053-230X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkclOwzAQhi0EgqrwAFxQJC5cCl6SuL4gVRVlEQKJRYKT5ThjCKR1sRNQbjwCz8iT4NBSsRy4eKyZ7_81C0KbBO8SgvneJcUJowzfUIIxiQVfQp021Wtzy9_-a2jD-wccoCAjXKyiNcZSijHrd9Bo6BpfqTLylat1VTuIrImUhsq2T1O-v74N7SBykIey8hAZZ8fRRaEfoap8oSIDZeHX0YpRpYeNeeyi69HB1fCod3p-eDwcnPZ0zGLaUzrhOs41I30WG5NDCkma09iAESJLOMvyhOea5KDSVHNhWJbFfWAcY5NpblgX7c98p3U2hlzDpHKqlFNXjJVrpFWF_FmZFPfyzj5LLjAWNA0GO3MDZ59q8JUcF15DWaoJ2NpLGgcqJQzTgG7_Qh9s7SZhvE8qrFYwHCgyo7Sz3jswi2YIlu3G5Z9DBc3W9ykWiq-zBEDMgJeihOZ_Rzm4HdGzk6Rt-wOYQaBu</recordid><startdate>202102</startdate><enddate>202102</enddate><creator>Rodarte, Justas V.</creator><creator>Abendroth, Jan</creator><creator>Edwards, Thomas E.</creator><creator>Lorimer, Donald D.</creator><creator>Staker, Bart L.</creator><creator>Zhang, Sunny</creator><creator>Myler, Peter J.</creator><creator>McLaughlin, Krystle J.</creator><general>International Union of Crystallography</general><general>Wiley Subscription Services, Inc</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>7QL</scope><scope>7T7</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-7497-3206</orcidid></search><sort><creationdate>202102</creationdate><title>Crystal structure of acetoacetyl‐CoA reductase from Rickettsia felis</title><author>Rodarte, Justas V. ; 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Section F, Structural biology communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rodarte, Justas V.</au><au>Abendroth, Jan</au><au>Edwards, Thomas E.</au><au>Lorimer, Donald D.</au><au>Staker, Bart L.</au><au>Zhang, Sunny</au><au>Myler, Peter J.</au><au>McLaughlin, Krystle J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal structure of acetoacetyl‐CoA reductase from Rickettsia felis</atitle><jtitle>Acta crystallographica. Section F, Structural biology communications</jtitle><addtitle>Acta Crystallogr F Struct Biol Commun</addtitle><date>2021-02</date><risdate>2021</risdate><volume>77</volume><issue>2</issue><spage>54</spage><epage>60</epage><pages>54-60</pages><issn>2053-230X</issn><eissn>2053-230X</eissn><abstract>Rickettsia felis, a Gram‐negative bacterium that causes spotted fever, is of increasing interest as an emerging human pathogen. R. felis and several other Rickettsia strains are classed as National Institute of Allergy and Infectious Diseases priority pathogens. In recent years, R. felis has been shown to be adaptable to a wide range of hosts, and many fevers of unknown origin are now being attributed to this infectious agent. Here, the structure of acetoacetyl‐CoA reductase from R. felis is reported at a resolution of 2.0 Å. While R. felis acetoacetyl‐CoA reductase shares less than 50% sequence identity with its closest homologs, it adopts a fold common to other short‐chain dehydrogenase/reductase (SDR) family members, such as the fatty‐acid synthesis II enzyme FabG from the prominent pathogens Staphylococcus aureus and Bacillus anthracis. Continued characterization of the Rickettsia proteome may prove to be an effective means of finding new avenues of treatment through comparative structural studies.
The structure of acetoacetyl‐CoA reductase from Rickettsia felis, the causative agent of flea‐borne spotted fever, is reported. Acetoacetyl‐CoA reductase is a key enzyme in both the glyoxylate/dicarboxylate and butanoate metabolic pathways.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>International Union of Crystallography</pub><pmid>33620038</pmid><doi>10.1107/S2053230X21001497</doi><tpages>7</tpages><orcidid>https://orcid.org/0000-0002-7497-3206</orcidid></addata></record> |
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subjects | acetoacetyl‐CoA reductase Alcohol Oxidoreductases - chemistry Alcohol Oxidoreductases - genetics Alcohol Oxidoreductases - isolation & purification Alcohol Oxidoreductases - metabolism Allergies Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - isolation & purification Bacterial Proteins - metabolism Crystal structure Crystallography, X-Ray Fever Homology Infectious diseases Models, Molecular oxidoreductase Pathogens PhaB Protein Conformation Proteomes Reductase Reductases Research Communications Rickettsia Rickettsia felis Rickettsia felis - enzymology Seattle Structural Genomics Center for Infectious Disease SSGCID structural genomics |
title | Crystal structure of acetoacetyl‐CoA reductase from Rickettsia felis |
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