Neutron and Atomic Resolution X‑ray Structures of a Lytic Polysaccharide Monooxygenase Reveal Copper-Mediated Dioxygen Binding and Evidence for N‑Terminal Deprotonation
A 1.1 Å resolution, room-temperature X-ray structure and a 2.1 Å resolution neutron structure of a chitin-degrading lytic polysaccharide monooxygenase domain from the bacterium Jonesia denitrificans (JdLPMO10A) show a putative dioxygen species equatorially bound to the active site copper. Both struc...
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| Veröffentlicht in: | Biochemistry (Easton) 2017-05, Vol.56 (20), p.2529-2532 |
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| container_title | Biochemistry (Easton) |
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| creator | Bacik, John-Paul Mekasha, Sophanit Forsberg, Zarah Kovalevsky, Andrey Y Vaaje-Kolstad, Gustav Eijsink, Vincent G. H Nix, Jay C Coates, Leighton Cuneo, Matthew J Unkefer, Clifford J Chen, Julian C.-H |
| description | A 1.1 Å resolution, room-temperature X-ray structure and a 2.1 Å resolution neutron structure of a chitin-degrading lytic polysaccharide monooxygenase domain from the bacterium Jonesia denitrificans (JdLPMO10A) show a putative dioxygen species equatorially bound to the active site copper. Both structures show an elongated density for the dioxygen, most consistent with a Cu(II)-bound peroxide. The coordination environment is consistent with Cu(II). In the neutron and X-ray structures, difference maps reveal the N-terminal amino group, involved in copper coordination, is present as a mixed ND2 and ND–, suggesting a role for the copper ion in shifting the pK a of the amino terminus. |
| doi_str_mv | 10.1021/acs.biochem.7b00019 |
| format | Article |
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The coordination environment is consistent with Cu(II). In the neutron and X-ray structures, difference maps reveal the N-terminal amino group, involved in copper coordination, is present as a mixed ND2 and ND–, suggesting a role for the copper ion in shifting the pK a of the amino terminus.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/acs.biochem.7b00019</identifier><identifier>PMID: 28481095</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>BASIC BIOLOGICAL SCIENCES ; biofuel neutron crystallography structure protein enzyme ; Biological Science ; Catalytic Domain ; Copper - chemistry ; Crystallography, X-Ray ; INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY ; Mixed Function Oxygenases - chemistry ; Oxygen - chemistry ; Polysaccharides - chemistry ; Protein Conformation ; Protons</subject><ispartof>Biochemistry (Easton), 2017-05, Vol.56 (20), p.2529-2532</ispartof><rights>Copyright © 2017 American Chemical Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a417t-a6173836b710cbb1bc736a86b39a97971213fedb1b2d3269de15062c45d862ff3</citedby><cites>FETCH-LOGICAL-a417t-a6173836b710cbb1bc736a86b39a97971213fedb1b2d3269de15062c45d862ff3</cites><orcidid>0000-0003-0341-165X ; 0000-0003-4459-9142 ; 0000000344599142 ; 0000000214756656 ; 000000030341165X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/acs.biochem.7b00019$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/acs.biochem.7b00019$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>230,314,780,784,885,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28481095$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/servlets/purl/1376613$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Bacik, John-Paul</creatorcontrib><creatorcontrib>Mekasha, Sophanit</creatorcontrib><creatorcontrib>Forsberg, Zarah</creatorcontrib><creatorcontrib>Kovalevsky, Andrey Y</creatorcontrib><creatorcontrib>Vaaje-Kolstad, Gustav</creatorcontrib><creatorcontrib>Eijsink, Vincent G. 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Both structures show an elongated density for the dioxygen, most consistent with a Cu(II)-bound peroxide. The coordination environment is consistent with Cu(II). In the neutron and X-ray structures, difference maps reveal the N-terminal amino group, involved in copper coordination, is present as a mixed ND2 and ND–, suggesting a role for the copper ion in shifting the pK a of the amino terminus.</description><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>biofuel neutron crystallography structure protein enzyme</subject><subject>Biological Science</subject><subject>Catalytic Domain</subject><subject>Copper - chemistry</subject><subject>Crystallography, X-Ray</subject><subject>INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY</subject><subject>Mixed Function Oxygenases - chemistry</subject><subject>Oxygen - chemistry</subject><subject>Polysaccharides - chemistry</subject><subject>Protein Conformation</subject><subject>Protons</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc1u1DAUhS0EokPhCZCQxYpNpv5JnHhZpqUgTQuCIrGzHOem4yqxp7ZTkV1fgffgqXgSPMzAkpXl6--cc-WD0EtKlpQweqJNXLbWmw2My7olhFD5CC1oxUhRSlk9Ros8EwWTghyhZzHe5mtJ6vIpOmJN2VAiqwX6eQVTCt5h7Tp8mvxoDf4M0Q9Tsnn67dfDj6Bn_CWFyaQpQMS-xxqv55TBT36YozZmo4PtAF965_33-QacjpBd7kEPeOW3WwjFJXRWJ-jwmd0j-K11nXU3f4LP77PeGcC9D_gqZ15DGK3L8jPYBp-807t1nqMnvR4ivDicx-jru_Pr1fti_fHiw-p0XeiS1qnQgta84aKtKTFtS1tTc6Eb0XKpZS1ryijvocsPrONMyA5oRQQzZdU1gvU9P0av974-JquisQnMxnjnwCRFeS0E5Rl6s4fygncTxKRGGw0Mg3bgp6hoI0VJy0qyjPI9aoKPMUCvtsGOOsyKErXrUuUu1aFLdegyq14dAqZ2hO6f5m95GTjZAzv1rZ9C_rD4X8vfB-Ox7A</recordid><startdate>20170523</startdate><enddate>20170523</enddate><creator>Bacik, John-Paul</creator><creator>Mekasha, Sophanit</creator><creator>Forsberg, Zarah</creator><creator>Kovalevsky, Andrey Y</creator><creator>Vaaje-Kolstad, Gustav</creator><creator>Eijsink, Vincent G. 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Both structures show an elongated density for the dioxygen, most consistent with a Cu(II)-bound peroxide. The coordination environment is consistent with Cu(II). In the neutron and X-ray structures, difference maps reveal the N-terminal amino group, involved in copper coordination, is present as a mixed ND2 and ND–, suggesting a role for the copper ion in shifting the pK a of the amino terminus.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>28481095</pmid><doi>10.1021/acs.biochem.7b00019</doi><tpages>4</tpages><orcidid>https://orcid.org/0000-0003-0341-165X</orcidid><orcidid>https://orcid.org/0000-0003-4459-9142</orcidid><orcidid>https://orcid.org/0000000344599142</orcidid><orcidid>https://orcid.org/0000000214756656</orcidid><orcidid>https://orcid.org/000000030341165X</orcidid><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | BASIC BIOLOGICAL SCIENCES biofuel neutron crystallography structure protein enzyme Biological Science Catalytic Domain Copper - chemistry Crystallography, X-Ray INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY Mixed Function Oxygenases - chemistry Oxygen - chemistry Polysaccharides - chemistry Protein Conformation Protons |
| title | Neutron and Atomic Resolution X‑ray Structures of a Lytic Polysaccharide Monooxygenase Reveal Copper-Mediated Dioxygen Binding and Evidence for N‑Terminal Deprotonation |
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