X‐ray crystallographic structure of BshB, the zinc‐dependent deacetylase involved in bacillithiol biosynthesis
Many gram‐positive bacteria produce bacillithiol to aid in the maintenance of redox homeostasis and degradation of toxic compounds, including the antibiotic fosfomycin. Bacillithiol is produced via a three‐enzyme pathway that includes the action of the zinc‐dependent deacetylase BshB. Previous studi...
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| Veröffentlicht in: | Protein science 2020-04, Vol.29 (4), p.1035-1039 |
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| creator | Woodward, Robert L. Castleman, Michaela M. Meloche, Chelsea E. Karpen, Mary E. Carlson, Clare G. Yobi, William H. Jepsen, Jacqueline C. Lewis, Benjamin W. Zarnosky, Brooke N. Cook, Paul D. |
| description | Many gram‐positive bacteria produce bacillithiol to aid in the maintenance of redox homeostasis and degradation of toxic compounds, including the antibiotic fosfomycin. Bacillithiol is produced via a three‐enzyme pathway that includes the action of the zinc‐dependent deacetylase BshB. Previous studies identified conserved aspartate and histidine residues within the active site that are involved in metal binding and catalysis, but the enzymatic mechanism is not fully understood. Here we report two X‐ray crystallographic structures of BshB from Bacillus subtilis that provide insight into the BshB catalytic mechanism.
PDB Code(s): 6P2T, 6ULL |
| doi_str_mv | 10.1002/pro.3808 |
| format | Article |
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PDB Code(s): 6P2T, 6ULL</description><identifier>ISSN: 0961-8368</identifier><identifier>EISSN: 1469-896X</identifier><identifier>DOI: 10.1002/pro.3808</identifier><identifier>PMID: 31867856</identifier><language>eng</language><publisher>Hoboken, USA: John Wiley & Sons, Inc</publisher><subject>Amidohydrolases - chemistry ; Amidohydrolases - metabolism ; Antibiotics ; Bacillithiol ; Bacillus subtilis - enzymology ; Bacterial Proteins - chemistry ; Bacterial Proteins - metabolism ; Biocatalysis ; Biodegradation ; Biosynthesis ; Catalysis ; Crystal structure ; Crystallography ; Crystallography, X-Ray ; Cysteine - analogs & derivatives ; Cysteine - biosynthesis ; Cysteine - chemistry ; deacetylase ; Fosfomycin ; Glucosamine - analogs & derivatives ; Glucosamine - biosynthesis ; Glucosamine - chemistry ; gram‐positive ; Histidine ; Homeostasis ; low‐molecular‐weight thiol ; Models, Molecular ; Protein Conformation ; Protein Structure Reports ; X‐ray crystallography ; Zinc ; Zinc - chemistry ; Zinc - metabolism</subject><ispartof>Protein science, 2020-04, Vol.29 (4), p.1035-1039</ispartof><rights>2019 The Protein Society</rights><rights>2019 The Protein Society.</rights><rights>2020 The Protein Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4658-74b8c420808679853dfb978de2ccf9fda0dc3f11fc2846801c67478860ea00793</citedby><cites>FETCH-LOGICAL-c4658-74b8c420808679853dfb978de2ccf9fda0dc3f11fc2846801c67478860ea00793</cites><orcidid>0000-0002-7286-2860 ; 0000000272862860</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/PMC7096702/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7096702/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,1411,1427,27901,27902,45550,45551,46384,46808,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31867856$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/1615848$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Woodward, Robert L.</creatorcontrib><creatorcontrib>Castleman, Michaela M.</creatorcontrib><creatorcontrib>Meloche, Chelsea E.</creatorcontrib><creatorcontrib>Karpen, Mary E.</creatorcontrib><creatorcontrib>Carlson, Clare G.</creatorcontrib><creatorcontrib>Yobi, William H.</creatorcontrib><creatorcontrib>Jepsen, Jacqueline C.</creatorcontrib><creatorcontrib>Lewis, Benjamin W.</creatorcontrib><creatorcontrib>Zarnosky, Brooke N.</creatorcontrib><creatorcontrib>Cook, Paul D.</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><title>X‐ray crystallographic structure of BshB, the zinc‐dependent deacetylase involved in bacillithiol biosynthesis</title><title>Protein science</title><addtitle>Protein Sci</addtitle><description>Many gram‐positive bacteria produce bacillithiol to aid in the maintenance of redox homeostasis and degradation of toxic compounds, including the antibiotic fosfomycin. Bacillithiol is produced via a three‐enzyme pathway that includes the action of the zinc‐dependent deacetylase BshB. Previous studies identified conserved aspartate and histidine residues within the active site that are involved in metal binding and catalysis, but the enzymatic mechanism is not fully understood. Here we report two X‐ray crystallographic structures of BshB from Bacillus subtilis that provide insight into the BshB catalytic mechanism.
PDB Code(s): 6P2T, 6ULL</description><subject>Amidohydrolases - chemistry</subject><subject>Amidohydrolases - metabolism</subject><subject>Antibiotics</subject><subject>Bacillithiol</subject><subject>Bacillus subtilis - enzymology</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biocatalysis</subject><subject>Biodegradation</subject><subject>Biosynthesis</subject><subject>Catalysis</subject><subject>Crystal structure</subject><subject>Crystallography</subject><subject>Crystallography, X-Ray</subject><subject>Cysteine - analogs & derivatives</subject><subject>Cysteine - biosynthesis</subject><subject>Cysteine - chemistry</subject><subject>deacetylase</subject><subject>Fosfomycin</subject><subject>Glucosamine - analogs & derivatives</subject><subject>Glucosamine - biosynthesis</subject><subject>Glucosamine - chemistry</subject><subject>gram‐positive</subject><subject>Histidine</subject><subject>Homeostasis</subject><subject>low‐molecular‐weight thiol</subject><subject>Models, Molecular</subject><subject>Protein Conformation</subject><subject>Protein Structure Reports</subject><subject>X‐ray crystallography</subject><subject>Zinc</subject><subject>Zinc - chemistry</subject><subject>Zinc - metabolism</subject><issn>0961-8368</issn><issn>1469-896X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kc9qFTEUxoMo9loFn0CCblw4Nf9uJrMRbLFVKFREobuQOZPppKSTaZK5Mq58BJ-xT2Juby26cJUT8jtfvnM-hJ5TckAJYW-nGA64IuoBWlEhm0o18vwhWpFG0kpxqfbQk5QuCSGCMv4Y7XGqZK3WcoXi-c3PX9EsGOKSsvE-XEQzDQ5wynGGPEeLQ48P03D4BufB4h9uhNLS2cmOnR0z7qwBmxdvksVu3AS_sV0pcGvAee_y4ILHrQtpGUt_cukpetQbn-yzu3MffTv-8PXoY3V6dvLp6P1pBUKuVVWLVoFgpIwl60atede3Ta06ywD6pu8M6YD3lPbAlJCKUJC1qJWSxBpC6obvo3c73Wlur2wHxWw0Xk_RXZm46GCc_vdldIO-CBtdl73VhBWBlzuBkLLTCVy2MEAYRwtZU0nXSqgCvbr7JYbr2aasL8McxzKYZlyxhgnBt9TrHQUxpBRtf2-DEr2NsNyD3kZY0Bd_274H_2RWgGoHfHfeLv8V0p-_nN0K_gYfc6nT</recordid><startdate>202004</startdate><enddate>202004</enddate><creator>Woodward, Robert L.</creator><creator>Castleman, Michaela M.</creator><creator>Meloche, Chelsea E.</creator><creator>Karpen, Mary E.</creator><creator>Carlson, Clare G.</creator><creator>Yobi, William H.</creator><creator>Jepsen, Jacqueline C.</creator><creator>Lewis, Benjamin W.</creator><creator>Zarnosky, Brooke N.</creator><creator>Cook, Paul D.</creator><general>John Wiley & Sons, Inc</general><general>Wiley Subscription Services, Inc</general><general>The Protein Society</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>7QO</scope><scope>7T5</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>P64</scope><scope>RC3</scope><scope>OTOTI</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-7286-2860</orcidid><orcidid>https://orcid.org/0000000272862860</orcidid></search><sort><creationdate>202004</creationdate><title>X‐ray crystallographic structure of BshB, the zinc‐dependent deacetylase involved in bacillithiol biosynthesis</title><author>Woodward, Robert L. ; Castleman, Michaela M. ; Meloche, Chelsea E. ; Karpen, Mary E. ; Carlson, Clare G. ; Yobi, William H. ; Jepsen, Jacqueline C. ; Lewis, Benjamin W. ; Zarnosky, Brooke N. ; Cook, Paul D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4658-74b8c420808679853dfb978de2ccf9fda0dc3f11fc2846801c67478860ea00793</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Amidohydrolases - chemistry</topic><topic>Amidohydrolases - metabolism</topic><topic>Antibiotics</topic><topic>Bacillithiol</topic><topic>Bacillus subtilis - enzymology</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - metabolism</topic><topic>Biocatalysis</topic><topic>Biodegradation</topic><topic>Biosynthesis</topic><topic>Catalysis</topic><topic>Crystal structure</topic><topic>Crystallography</topic><topic>Crystallography, X-Ray</topic><topic>Cysteine - analogs & derivatives</topic><topic>Cysteine - biosynthesis</topic><topic>Cysteine - chemistry</topic><topic>deacetylase</topic><topic>Fosfomycin</topic><topic>Glucosamine - analogs & derivatives</topic><topic>Glucosamine - biosynthesis</topic><topic>Glucosamine - chemistry</topic><topic>gram‐positive</topic><topic>Histidine</topic><topic>Homeostasis</topic><topic>low‐molecular‐weight thiol</topic><topic>Models, Molecular</topic><topic>Protein Conformation</topic><topic>Protein Structure Reports</topic><topic>X‐ray crystallography</topic><topic>Zinc</topic><topic>Zinc - chemistry</topic><topic>Zinc - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Woodward, Robert L.</creatorcontrib><creatorcontrib>Castleman, Michaela M.</creatorcontrib><creatorcontrib>Meloche, Chelsea E.</creatorcontrib><creatorcontrib>Karpen, Mary E.</creatorcontrib><creatorcontrib>Carlson, Clare G.</creatorcontrib><creatorcontrib>Yobi, William H.</creatorcontrib><creatorcontrib>Jepsen, Jacqueline C.</creatorcontrib><creatorcontrib>Lewis, Benjamin W.</creatorcontrib><creatorcontrib>Zarnosky, Brooke N.</creatorcontrib><creatorcontrib>Cook, Paul D.</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Immunology Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Protein science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Woodward, Robert L.</au><au>Castleman, Michaela M.</au><au>Meloche, Chelsea E.</au><au>Karpen, Mary E.</au><au>Carlson, Clare G.</au><au>Yobi, William H.</au><au>Jepsen, Jacqueline C.</au><au>Lewis, Benjamin W.</au><au>Zarnosky, Brooke N.</au><au>Cook, Paul D.</au><aucorp>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>X‐ray crystallographic structure of BshB, the zinc‐dependent deacetylase involved in bacillithiol biosynthesis</atitle><jtitle>Protein science</jtitle><addtitle>Protein Sci</addtitle><date>2020-04</date><risdate>2020</risdate><volume>29</volume><issue>4</issue><spage>1035</spage><epage>1039</epage><pages>1035-1039</pages><issn>0961-8368</issn><eissn>1469-896X</eissn><abstract>Many gram‐positive bacteria produce bacillithiol to aid in the maintenance of redox homeostasis and degradation of toxic compounds, including the antibiotic fosfomycin. Bacillithiol is produced via a three‐enzyme pathway that includes the action of the zinc‐dependent deacetylase BshB. Previous studies identified conserved aspartate and histidine residues within the active site that are involved in metal binding and catalysis, but the enzymatic mechanism is not fully understood. Here we report two X‐ray crystallographic structures of BshB from Bacillus subtilis that provide insight into the BshB catalytic mechanism.
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| subjects | Amidohydrolases - chemistry Amidohydrolases - metabolism Antibiotics Bacillithiol Bacillus subtilis - enzymology Bacterial Proteins - chemistry Bacterial Proteins - metabolism Biocatalysis Biodegradation Biosynthesis Catalysis Crystal structure Crystallography Crystallography, X-Ray Cysteine - analogs & derivatives Cysteine - biosynthesis Cysteine - chemistry deacetylase Fosfomycin Glucosamine - analogs & derivatives Glucosamine - biosynthesis Glucosamine - chemistry gram‐positive Histidine Homeostasis low‐molecular‐weight thiol Models, Molecular Protein Conformation Protein Structure Reports X‐ray crystallography Zinc Zinc - chemistry Zinc - metabolism |
| title | X‐ray crystallographic structure of BshB, the zinc‐dependent deacetylase involved in bacillithiol biosynthesis |
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