Structural Basis for Target Protein Recognition by the Protein Disulfide Reductase Thioredoxin
Thioredoxin is ubiquitous and regulates various target proteins through disulfide bond reduction. We report the structure of thioredoxin (HvTrxh2 from barley) in a reaction intermediate complex with a protein substrate, barley α-amylase/subtilisin inhibitor (BASI). The crystal structure of this mixe...
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| Veröffentlicht in: | Structure (London) 2006-11, Vol.14 (11), p.1701-1710 |
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| creator | Maeda, Kenji Hägglund, Per Finnie, Christine Svensson, Birte Henriksen, Anette |
| description | Thioredoxin is ubiquitous and regulates various target proteins through disulfide bond reduction. We report the structure of thioredoxin (HvTrxh2 from barley) in a reaction intermediate complex with a protein substrate, barley α-amylase/subtilisin inhibitor (BASI). The crystal structure of this mixed disulfide shows a conserved hydrophobic motif in thioredoxin interacting with a sequence of residues from BASI through van der Waals contacts and backbone-backbone hydrogen bonds. The observed structural complementarity suggests that the recognition of features around protein disulfides plays a major role in the specificity and protein disulfide reductase activity of thioredoxin. This novel insight into the function of thioredoxin constitutes a basis for comprehensive understanding of its biological role. Moreover, comparison with structurally related proteins shows that thioredoxin shares a mechanism with glutaredoxin and glutathione transferase for correctly positioning substrate cysteine residues at the catalytic groups but possesses a unique structural element that allows recognition of protein disulfides. |
| doi_str_mv | 10.1016/j.str.2006.09.012 |
| format | Article |
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We report the structure of thioredoxin (HvTrxh2 from barley) in a reaction intermediate complex with a protein substrate, barley α-amylase/subtilisin inhibitor (BASI). The crystal structure of this mixed disulfide shows a conserved hydrophobic motif in thioredoxin interacting with a sequence of residues from BASI through van der Waals contacts and backbone-backbone hydrogen bonds. The observed structural complementarity suggests that the recognition of features around protein disulfides plays a major role in the specificity and protein disulfide reductase activity of thioredoxin. This novel insight into the function of thioredoxin constitutes a basis for comprehensive understanding of its biological role. Moreover, comparison with structurally related proteins shows that thioredoxin shares a mechanism with glutaredoxin and glutathione transferase for correctly positioning substrate cysteine residues at the catalytic groups but possesses a unique structural element that allows recognition of protein disulfides.</description><subject>Amino Acid Motifs</subject><subject>Crystallography, X-Ray</subject><subject>Cysteine - chemistry</subject><subject>Disulfides - chemistry</subject><subject>Glutaredoxins</subject><subject>Glutathione - chemistry</subject><subject>Glutathione Transferase - chemistry</subject><subject>Glutathione Transferase - metabolism</subject><subject>Hordeum</subject><subject>Models, Chemical</subject><subject>Models, Molecular</subject><subject>Molecular Conformation</subject><subject>Oxidoreductases - chemistry</subject><subject>Protein Disulfide Reductase (Glutathione) - chemistry</subject><subject>Protein Folding</subject><subject>PROTEINS</subject><subject>Proteins - chemistry</subject><subject>Thioredoxins - chemistry</subject><issn>0969-2126</issn><issn>1878-4186</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kLtu3DAQRYkghr1-fECaQFU6yUNKokikStZPwECCZF0TFDmyudCKDkkZ9t_kW_xlobGLuHM1xZx7MXMI-UShokD56bqKKVQMgFcgK6DsA1lQ0YmyoYJ_JAuQXJaMMn5ADmNcAwBrAfbJAe1ACirbBVG_U5hNmoMei-86ulgMPhQrHe4wFT-DT-im4hcafze55PxU9M8vf9M9_t-duTiPg7OYKZubdMRide98QOuf3HRM9gY9RjzZzSNye3G-Wl6VNz8ur5ffbkrTcEhlz1gna2i5reXQNz3m83grsRYNtIYOommFFQ3T0Na01n1XI0rbSWEZxaHt6iPyZdv7EPyfGWNSGxcNjqOe0M9RcUFrThvIIN2CJvgYAw7qIbiNDs-Kgnq1qtYqW1WvVhVIla3mzOdd-dxv0L4ldhoz8HULYH7x0WFQ0TicDFoX0CRlvXun_h_npIk5</recordid><startdate>20061101</startdate><enddate>20061101</enddate><creator>Maeda, Kenji</creator><creator>Hägglund, Per</creator><creator>Finnie, Christine</creator><creator>Svensson, Birte</creator><creator>Henriksen, Anette</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><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></search><sort><creationdate>20061101</creationdate><title>Structural Basis for Target Protein Recognition by the Protein Disulfide Reductase Thioredoxin</title><author>Maeda, Kenji ; Hägglund, Per ; Finnie, Christine ; Svensson, Birte ; Henriksen, Anette</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c460t-b22793056d39fb4be981659e38405c1f8458d842a05313ab73ee9d798d21ef573</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Amino Acid Motifs</topic><topic>Crystallography, X-Ray</topic><topic>Cysteine - chemistry</topic><topic>Disulfides - chemistry</topic><topic>Glutaredoxins</topic><topic>Glutathione - chemistry</topic><topic>Glutathione Transferase - chemistry</topic><topic>Glutathione Transferase - metabolism</topic><topic>Hordeum</topic><topic>Models, Chemical</topic><topic>Models, Molecular</topic><topic>Molecular Conformation</topic><topic>Oxidoreductases - chemistry</topic><topic>Protein Disulfide Reductase (Glutathione) - chemistry</topic><topic>Protein Folding</topic><topic>PROTEINS</topic><topic>Proteins - chemistry</topic><topic>Thioredoxins - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Maeda, Kenji</creatorcontrib><creatorcontrib>Hägglund, Per</creatorcontrib><creatorcontrib>Finnie, Christine</creatorcontrib><creatorcontrib>Svensson, Birte</creatorcontrib><creatorcontrib>Henriksen, Anette</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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><jtitle>Structure (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Maeda, Kenji</au><au>Hägglund, Per</au><au>Finnie, Christine</au><au>Svensson, Birte</au><au>Henriksen, Anette</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural Basis for Target Protein Recognition by the Protein Disulfide Reductase Thioredoxin</atitle><jtitle>Structure (London)</jtitle><addtitle>Structure</addtitle><date>2006-11-01</date><risdate>2006</risdate><volume>14</volume><issue>11</issue><spage>1701</spage><epage>1710</epage><pages>1701-1710</pages><issn>0969-2126</issn><eissn>1878-4186</eissn><abstract>Thioredoxin is ubiquitous and regulates various target proteins through disulfide bond reduction. We report the structure of thioredoxin (HvTrxh2 from barley) in a reaction intermediate complex with a protein substrate, barley α-amylase/subtilisin inhibitor (BASI). The crystal structure of this mixed disulfide shows a conserved hydrophobic motif in thioredoxin interacting with a sequence of residues from BASI through van der Waals contacts and backbone-backbone hydrogen bonds. The observed structural complementarity suggests that the recognition of features around protein disulfides plays a major role in the specificity and protein disulfide reductase activity of thioredoxin. This novel insight into the function of thioredoxin constitutes a basis for comprehensive understanding of its biological role. 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| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Cell Press Free Archives; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Motifs Crystallography, X-Ray Cysteine - chemistry Disulfides - chemistry Glutaredoxins Glutathione - chemistry Glutathione Transferase - chemistry Glutathione Transferase - metabolism Hordeum Models, Chemical Models, Molecular Molecular Conformation Oxidoreductases - chemistry Protein Disulfide Reductase (Glutathione) - chemistry Protein Folding PROTEINS Proteins - chemistry Thioredoxins - chemistry |
| title | Structural Basis for Target Protein Recognition by the Protein Disulfide Reductase Thioredoxin |
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