The X‐ray crystal structure of human A15C neuroglobin reveals both native/de novo disulfide bonds and unexpected ligand‐binding sites
Human neuroglobin (Ngb) contains a heme group and three Cys residues (Cys46, Cys55, and Cys120) in the polypeptide chain. By introducing an additional Cys at position 15, the X‐ray structure of A15C Ngb mutant was solved at a high resolution of 1.35 Å, which reveals the formation of both the native...
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| Veröffentlicht in: | Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2022-05, Vol.90 (5), p.1152-1158 |
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| container_title | Proteins, structure, function, and bioinformatics |
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| creator | Gao, Shu‐Qin Yuan, Hong Liu, Xi‐Chun Li, Lianzhi Tan, Xiangshi Wen, Ge‐Bo Lin, Ying‐Wu |
| description | Human neuroglobin (Ngb) contains a heme group and three Cys residues (Cys46, Cys55, and Cys120) in the polypeptide chain. By introducing an additional Cys at position 15, the X‐ray structure of A15C Ngb mutant was solved at a high resolution of 1.35 Å, which reveals the formation of both the native (C46C55) and the engineered (C15C120) disulfide bonds, likely playing a functional and structural role, respectively, according to the geometry analysis. Unexpectedly, 1,4‐dioxane from the crystallization reagents was bound not only to the protein surface, but also to the heme distal pocket, providing insights into protein‐ligand interactions for the globin and guiding the design of functional heme enzymes. |
| doi_str_mv | 10.1002/prot.26297 |
| format | Article |
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By introducing an additional Cys at position 15, the X‐ray structure of A15C Ngb mutant was solved at a high resolution of 1.35 Å, which reveals the formation of both the native (C46C55) and the engineered (C15C120) disulfide bonds, likely playing a functional and structural role, respectively, according to the geometry analysis. Unexpectedly, 1,4‐dioxane from the crystallization reagents was bound not only to the protein surface, but also to the heme distal pocket, providing insights into protein‐ligand interactions for the globin and guiding the design of functional heme enzymes.</description><identifier>ISSN: 0887-3585</identifier><identifier>EISSN: 1097-0134</identifier><identifier>DOI: 10.1002/prot.26297</identifier><identifier>PMID: 34982478</identifier><language>eng</language><publisher>Hoboken, USA: John Wiley & Sons, Inc</publisher><subject>Binding Sites ; Chemical bonds ; Crystal structure ; Crystallization ; disulfide bond ; Disulfide bonds ; Disulfides - chemistry ; globins ; Globins - chemistry ; Globins - genetics ; Globins - metabolism ; Heme ; Heme - chemistry ; Humans ; Ligands ; ligand‐binding site ; Nerve Tissue Proteins - chemistry ; Neuroglobin ; Polypeptides ; Proteins ; Reagents ; Structure-function relationships ; X-Rays ; X‐ray crystallography</subject><ispartof>Proteins, structure, function, and bioinformatics, 2022-05, Vol.90 (5), p.1152-1158</ispartof><rights>2022 Wiley Periodicals LLC.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2877-3cd9ac6a78a10ab33feab712d69187cca40adae52d69fff207155e5a9ea3e3953</citedby><cites>FETCH-LOGICAL-c2877-3cd9ac6a78a10ab33feab712d69187cca40adae52d69fff207155e5a9ea3e3953</cites><orcidid>0000-0002-2457-0871</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fprot.26297$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fprot.26297$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34982478$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gao, Shu‐Qin</creatorcontrib><creatorcontrib>Yuan, Hong</creatorcontrib><creatorcontrib>Liu, Xi‐Chun</creatorcontrib><creatorcontrib>Li, Lianzhi</creatorcontrib><creatorcontrib>Tan, Xiangshi</creatorcontrib><creatorcontrib>Wen, Ge‐Bo</creatorcontrib><creatorcontrib>Lin, Ying‐Wu</creatorcontrib><title>The X‐ray crystal structure of human A15C neuroglobin reveals both native/de novo disulfide bonds and unexpected ligand‐binding sites</title><title>Proteins, structure, function, and bioinformatics</title><addtitle>Proteins</addtitle><description>Human neuroglobin (Ngb) contains a heme group and three Cys residues (Cys46, Cys55, and Cys120) in the polypeptide chain. 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| subjects | Binding Sites Chemical bonds Crystal structure Crystallization disulfide bond Disulfide bonds Disulfides - chemistry globins Globins - chemistry Globins - genetics Globins - metabolism Heme Heme - chemistry Humans Ligands ligand‐binding site Nerve Tissue Proteins - chemistry Neuroglobin Polypeptides Proteins Reagents Structure-function relationships X-Rays X‐ray crystallography |
| title | The X‐ray crystal structure of human A15C neuroglobin reveals both native/de novo disulfide bonds and unexpected ligand‐binding sites |
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