Crystal structure of the NADP-dependent mannitol dehydrogenase from Cladosporium herbarum: Implications for oligomerisation and catalysis
The ascomycete Cladosporium herbarum is a prominent fungal inducer of Type I allergy. The only major allergen identified so far is Cla h 8, a NADP-dependent mannitol dehydrogenase (MtDH). MtDH, a cytoplasmic protein of 28.5 kDa, belongs to the Short chain Dehydrogenases/ Reductases (SDR), acting as...
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| Veröffentlicht in: | Biochimie 2010-08, Vol.92 (8), p.985-993 |
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| creator | Nüss, Dorota Goettig, Peter Magler, Iris Denk, Ursula Breitenbach, Michael Schneider, Peter B. Brandstetter, Hans Simon-Nobbe, Birgit |
| description | The ascomycete
Cladosporium herbarum is a prominent fungal inducer of Type I allergy. The only major allergen identified so far is Cla h 8, a NADP-dependent mannitol dehydrogenase (MtDH). MtDH, a cytoplasmic protein of 28.5
kDa, belongs to the
Short chain
Dehydrogenases/
Reductases (SDR), acting as a NADP-dependent oxidoreductase.
In this study, we found that
C. herbarum MtDH can exist as monomers, dimers and tetramers in solution and, correspondingly, forms tetramers and higher oligomers in two crystal structures. Additionally, we identified a unique adaptive binding site for the metal ions Na
+ and Zn
2+ that were distinguished by an anomalous dispersion experiment. A Translation-Libration-Screw analysis confirmed the stabilising effect of Zn
2+ for the tetrameric assembly. Moreover, the zinc containing structure explains the mode of MtDH multimerisation by metal bridging of the tetramers. The formation of oligomers and higher multimers of MtDH provides a missing link to its allergenic properties. Based on the well defined active site region and a comparative analysis with related structures, we can also clarify the atypical enzymatic properties of MtDH by two alternative binding modes of the substrate to the active site. |
| doi_str_mv | 10.1016/j.biochi.2010.04.012 |
| format | Article |
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Cladosporium herbarum is a prominent fungal inducer of Type I allergy. The only major allergen identified so far is Cla h 8, a NADP-dependent mannitol dehydrogenase (MtDH). MtDH, a cytoplasmic protein of 28.5
kDa, belongs to the
Short chain
Dehydrogenases/
Reductases (SDR), acting as a NADP-dependent oxidoreductase.
In this study, we found that
C. herbarum MtDH can exist as monomers, dimers and tetramers in solution and, correspondingly, forms tetramers and higher oligomers in two crystal structures. Additionally, we identified a unique adaptive binding site for the metal ions Na
+ and Zn
2+ that were distinguished by an anomalous dispersion experiment. A Translation-Libration-Screw analysis confirmed the stabilising effect of Zn
2+ for the tetrameric assembly. Moreover, the zinc containing structure explains the mode of MtDH multimerisation by metal bridging of the tetramers. The formation of oligomers and higher multimers of MtDH provides a missing link to its allergenic properties. Based on the well defined active site region and a comparative analysis with related structures, we can also clarify the atypical enzymatic properties of MtDH by two alternative binding modes of the substrate to the active site.</description><identifier>ISSN: 0300-9084</identifier><identifier>EISSN: 1638-6183</identifier><identifier>DOI: 10.1016/j.biochi.2010.04.012</identifier><identifier>PMID: 20420880</identifier><language>eng</language><publisher>France: Elsevier Masson SAS</publisher><subject>Allergens ; Amino Acid Sequence ; Ascomycetes ; Biocatalysis ; Biopolymers - chemistry ; Biopolymers - metabolism ; Catalysis ; Cladosporium - enzymology ; Crystal structure ; Crystallography, X-Ray ; Kinetics ; Mannitol dehydrogenase ; Mannitol Dehydrogenases - chemistry ; Mannitol Dehydrogenases - isolation & purification ; Mannitol Dehydrogenases - metabolism ; Models, Molecular ; Molecular Sequence Data ; Oligomer ; Protein Conformation ; Reductase ; Sequence Homology, Amino Acid</subject><ispartof>Biochimie, 2010-08, Vol.92 (8), p.985-993</ispartof><rights>2010 Elsevier Masson SAS</rights><rights>Copyright 2010 Elsevier Masson SAS. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c393t-605d9f79e052d187e53f12379c2a2d11690969b097a53ae13060deab9fc624623</citedby><cites>FETCH-LOGICAL-c393t-605d9f79e052d187e53f12379c2a2d11690969b097a53ae13060deab9fc624623</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.biochi.2010.04.012$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20420880$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nüss, Dorota</creatorcontrib><creatorcontrib>Goettig, Peter</creatorcontrib><creatorcontrib>Magler, Iris</creatorcontrib><creatorcontrib>Denk, Ursula</creatorcontrib><creatorcontrib>Breitenbach, Michael</creatorcontrib><creatorcontrib>Schneider, Peter B.</creatorcontrib><creatorcontrib>Brandstetter, Hans</creatorcontrib><creatorcontrib>Simon-Nobbe, Birgit</creatorcontrib><title>Crystal structure of the NADP-dependent mannitol dehydrogenase from Cladosporium herbarum: Implications for oligomerisation and catalysis</title><title>Biochimie</title><addtitle>Biochimie</addtitle><description>The ascomycete
Cladosporium herbarum is a prominent fungal inducer of Type I allergy. The only major allergen identified so far is Cla h 8, a NADP-dependent mannitol dehydrogenase (MtDH). MtDH, a cytoplasmic protein of 28.5
kDa, belongs to the
Short chain
Dehydrogenases/
Reductases (SDR), acting as a NADP-dependent oxidoreductase.
In this study, we found that
C. herbarum MtDH can exist as monomers, dimers and tetramers in solution and, correspondingly, forms tetramers and higher oligomers in two crystal structures. Additionally, we identified a unique adaptive binding site for the metal ions Na
+ and Zn
2+ that were distinguished by an anomalous dispersion experiment. A Translation-Libration-Screw analysis confirmed the stabilising effect of Zn
2+ for the tetrameric assembly. Moreover, the zinc containing structure explains the mode of MtDH multimerisation by metal bridging of the tetramers. The formation of oligomers and higher multimers of MtDH provides a missing link to its allergenic properties. Based on the well defined active site region and a comparative analysis with related structures, we can also clarify the atypical enzymatic properties of MtDH by two alternative binding modes of the substrate to the active site.</description><subject>Allergens</subject><subject>Amino Acid Sequence</subject><subject>Ascomycetes</subject><subject>Biocatalysis</subject><subject>Biopolymers - chemistry</subject><subject>Biopolymers - metabolism</subject><subject>Catalysis</subject><subject>Cladosporium - enzymology</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>Kinetics</subject><subject>Mannitol dehydrogenase</subject><subject>Mannitol Dehydrogenases - chemistry</subject><subject>Mannitol Dehydrogenases - isolation & purification</subject><subject>Mannitol Dehydrogenases - metabolism</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Oligomer</subject><subject>Protein Conformation</subject><subject>Reductase</subject><subject>Sequence Homology, Amino Acid</subject><issn>0300-9084</issn><issn>1638-6183</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9u1DAQhy0EokvhDRDyjVOWsZ04MQekavlXqWo5wNly7EnXKycOtoO0j8Bbk7Klx3Ia6TffzEjzEfKawZYBk-8O295Hu_dbDmsE9RYYf0I2TIqukqwTT8kGBECloKvPyIucDwDQAFfPyRmHmkPXwYb83qVjLibQXNJiy5KQxoGWPdLri4_fKoczTg6nQkczTb7EQB3ujy7FW5xMRjqkONJdMC7mOSa_jHSPqTdpGd_Ty3EO3pri45TpEBONwd_GEZPPf0NqJkfXvgnH7PNL8mwwIeOr-3pOfnz-9H33tbq6-XK5u7iqrFCiVBIap4ZWITTcsa7FRgyMi1ZZbtaASQVKqh5UaxphkAmQ4ND0arCS15KLc_L2tHdO8eeCuejRZ4shmAnjkrViHQjZsfa_ZCtqAMGaZiXrE2lTzDnhoOfkR5OOmoG-s6UP-mRL39nSUOvV1jr25v7A0o_oHob-6VmBDycA14f88ph0th4ni84ntEW76B-_8Ad-Vqme</recordid><startdate>20100801</startdate><enddate>20100801</enddate><creator>Nüss, Dorota</creator><creator>Goettig, Peter</creator><creator>Magler, Iris</creator><creator>Denk, Ursula</creator><creator>Breitenbach, Michael</creator><creator>Schneider, Peter B.</creator><creator>Brandstetter, Hans</creator><creator>Simon-Nobbe, Birgit</creator><general>Elsevier Masson SAS</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><scope>M7N</scope></search><sort><creationdate>20100801</creationdate><title>Crystal structure of the NADP-dependent mannitol dehydrogenase from Cladosporium herbarum: Implications for oligomerisation and catalysis</title><author>Nüss, Dorota ; Goettig, Peter ; Magler, Iris ; Denk, Ursula ; Breitenbach, Michael ; Schneider, Peter B. ; Brandstetter, Hans ; Simon-Nobbe, Birgit</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c393t-605d9f79e052d187e53f12379c2a2d11690969b097a53ae13060deab9fc624623</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Allergens</topic><topic>Amino Acid Sequence</topic><topic>Ascomycetes</topic><topic>Biocatalysis</topic><topic>Biopolymers - chemistry</topic><topic>Biopolymers - metabolism</topic><topic>Catalysis</topic><topic>Cladosporium - enzymology</topic><topic>Crystal structure</topic><topic>Crystallography, X-Ray</topic><topic>Kinetics</topic><topic>Mannitol dehydrogenase</topic><topic>Mannitol Dehydrogenases - chemistry</topic><topic>Mannitol Dehydrogenases - isolation & purification</topic><topic>Mannitol Dehydrogenases - metabolism</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Oligomer</topic><topic>Protein Conformation</topic><topic>Reductase</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nüss, Dorota</creatorcontrib><creatorcontrib>Goettig, Peter</creatorcontrib><creatorcontrib>Magler, Iris</creatorcontrib><creatorcontrib>Denk, Ursula</creatorcontrib><creatorcontrib>Breitenbach, Michael</creatorcontrib><creatorcontrib>Schneider, Peter B.</creatorcontrib><creatorcontrib>Brandstetter, Hans</creatorcontrib><creatorcontrib>Simon-Nobbe, Birgit</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><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><jtitle>Biochimie</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nüss, Dorota</au><au>Goettig, Peter</au><au>Magler, Iris</au><au>Denk, Ursula</au><au>Breitenbach, Michael</au><au>Schneider, Peter B.</au><au>Brandstetter, Hans</au><au>Simon-Nobbe, Birgit</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal structure of the NADP-dependent mannitol dehydrogenase from Cladosporium herbarum: Implications for oligomerisation and catalysis</atitle><jtitle>Biochimie</jtitle><addtitle>Biochimie</addtitle><date>2010-08-01</date><risdate>2010</risdate><volume>92</volume><issue>8</issue><spage>985</spage><epage>993</epage><pages>985-993</pages><issn>0300-9084</issn><eissn>1638-6183</eissn><abstract>The ascomycete
Cladosporium herbarum is a prominent fungal inducer of Type I allergy. The only major allergen identified so far is Cla h 8, a NADP-dependent mannitol dehydrogenase (MtDH). MtDH, a cytoplasmic protein of 28.5
kDa, belongs to the
Short chain
Dehydrogenases/
Reductases (SDR), acting as a NADP-dependent oxidoreductase.
In this study, we found that
C. herbarum MtDH can exist as monomers, dimers and tetramers in solution and, correspondingly, forms tetramers and higher oligomers in two crystal structures. Additionally, we identified a unique adaptive binding site for the metal ions Na
+ and Zn
2+ that were distinguished by an anomalous dispersion experiment. A Translation-Libration-Screw analysis confirmed the stabilising effect of Zn
2+ for the tetrameric assembly. Moreover, the zinc containing structure explains the mode of MtDH multimerisation by metal bridging of the tetramers. The formation of oligomers and higher multimers of MtDH provides a missing link to its allergenic properties. Based on the well defined active site region and a comparative analysis with related structures, we can also clarify the atypical enzymatic properties of MtDH by two alternative binding modes of the substrate to the active site.</abstract><cop>France</cop><pub>Elsevier Masson SAS</pub><pmid>20420880</pmid><doi>10.1016/j.biochi.2010.04.012</doi><tpages>9</tpages></addata></record> |
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| ispartof | Biochimie, 2010-08, Vol.92 (8), p.985-993 |
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| subjects | Allergens Amino Acid Sequence Ascomycetes Biocatalysis Biopolymers - chemistry Biopolymers - metabolism Catalysis Cladosporium - enzymology Crystal structure Crystallography, X-Ray Kinetics Mannitol dehydrogenase Mannitol Dehydrogenases - chemistry Mannitol Dehydrogenases - isolation & purification Mannitol Dehydrogenases - metabolism Models, Molecular Molecular Sequence Data Oligomer Protein Conformation Reductase Sequence Homology, Amino Acid |
| title | Crystal structure of the NADP-dependent mannitol dehydrogenase from Cladosporium herbarum: Implications for oligomerisation and catalysis |
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