Structures of Thermoactinomyces vulgaris R-47 alpha-amylase II complexed with substrate analogues
The structures of Thermoactinomyces vulgaris R-47 α-amylase II mutant (d325nTVA II) complexed with substrate analogues, methyl β-cyclodextrin (mβ-CD) and maltohexaose (G6), were solved by X-ray diffraction at 3.2Å and 3.3Å resolution, respectively. In d325nTVA II-mβ-CD complex, the orientation and b...
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| Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2001-03, Vol.65 (3), p.619-626 |
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| creator | Yokota, T. (Tokyo Univ. of Agriculture and Technology, Fuchu (Japan)) Tonozuka, T Shimura, Y Ichikawa, K Kamitori, S Sakano, Y |
| description | The structures of Thermoactinomyces vulgaris R-47 α-amylase II mutant (d325nTVA II) complexed with substrate analogues, methyl β-cyclodextrin (mβ-CD) and maltohexaose (G6), were solved by X-ray diffraction at 3.2Å and 3.3Å resolution, respectively. In d325nTVA II-mβ-CD complex, the orientation and binding-position of β-CD in TVA II were identical to those in cyclodextin glucanotransferase (CGTase). The active site residues were essentialy conserved, while there are no residues corresponding to Tyr89, Phe183, and His233 of CGTase in TVA II. In d325nTVA II-G6 complex, the electron density maps of two glucosyl units at the non-reducing end were disordered and invisible. The four glucosyl units of G6 were bound to TVA II as in CGTase, while the others were not stacked and were probably flexible. The residues of TVA II corresponding to Tyr89, Lys232, and His233 of CGTase were completely lacking. These results suggest that the lack of the residues related to α-glucan and CD-stacking causes the functional distinctions between CGTase and TVA II. |
| doi_str_mv | 10.1271/bbb.65.619 |
| format | Article |
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(Tokyo Univ. of Agriculture and Technology, Fuchu (Japan)) ; Tonozuka, T ; Shimura, Y ; Ichikawa, K ; Kamitori, S ; Sakano, Y</creator><creatorcontrib>Yokota, T. (Tokyo Univ. of Agriculture and Technology, Fuchu (Japan)) ; Tonozuka, T ; Shimura, Y ; Ichikawa, K ; Kamitori, S ; Sakano, Y</creatorcontrib><description>The structures of Thermoactinomyces vulgaris R-47 α-amylase II mutant (d325nTVA II) complexed with substrate analogues, methyl β-cyclodextrin (mβ-CD) and maltohexaose (G6), were solved by X-ray diffraction at 3.2Å and 3.3Å resolution, respectively. In d325nTVA II-mβ-CD complex, the orientation and binding-position of β-CD in TVA II were identical to those in cyclodextin glucanotransferase (CGTase). The active site residues were essentialy conserved, while there are no residues corresponding to Tyr89, Phe183, and His233 of CGTase in TVA II. In d325nTVA II-G6 complex, the electron density maps of two glucosyl units at the non-reducing end were disordered and invisible. The four glucosyl units of G6 were bound to TVA II as in CGTase, while the others were not stacked and were probably flexible. The residues of TVA II corresponding to Tyr89, Lys232, and His233 of CGTase were completely lacking. These results suggest that the lack of the residues related to α-glucan and CD-stacking causes the functional distinctions between CGTase and TVA II.</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1271/bbb.65.619</identifier><identifier>PMID: 11330677</identifier><language>eng</language><publisher>Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry</publisher><subject>a-Amylase II ; ALPHA AMYLASE ; alpha-Amylases - chemistry ; alpha-Amylases - physiology ; Analytical, structural and metabolic biochemistry ; b-Glucan ; beta-Cyclodextrins ; Biological and medical sciences ; CHEMICAL STRUCTURE ; crystal structure ; Cyclodextrins - chemistry ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Glucosyltransferases - chemistry ; Hydrolases ; methyl ^b-cyclodextrin ; Micromonosporaceae - enzymology ; Models, Molecular ; Oligosaccharides - chemistry ; Protein Structure, Tertiary ; pullulan ; Substrate Specificity ; THERMOACTINOMYCES ; Thermoactinomyces vulgaris ; TVA II ; α-amylase</subject><ispartof>Bioscience, biotechnology, and biochemistry, 2001-03, Vol.65 (3), p.619-626</ispartof><rights>2001 by Japan Society for Bioscience, Biotechnology, and Agrochemistry 2001</rights><rights>2001 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c477t-cc89f1e9303c8ecdca2305305af5dd83bb868707374a5c0f49157db7da7f887e3</citedby><cites>FETCH-LOGICAL-c477t-cc89f1e9303c8ecdca2305305af5dd83bb868707374a5c0f49157db7da7f887e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1129336$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11330677$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yokota, T. (Tokyo Univ. of Agriculture and Technology, Fuchu (Japan))</creatorcontrib><creatorcontrib>Tonozuka, T</creatorcontrib><creatorcontrib>Shimura, Y</creatorcontrib><creatorcontrib>Ichikawa, K</creatorcontrib><creatorcontrib>Kamitori, S</creatorcontrib><creatorcontrib>Sakano, Y</creatorcontrib><title>Structures of Thermoactinomyces vulgaris R-47 alpha-amylase II complexed with substrate analogues</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>The structures of Thermoactinomyces vulgaris R-47 α-amylase II mutant (d325nTVA II) complexed with substrate analogues, methyl β-cyclodextrin (mβ-CD) and maltohexaose (G6), were solved by X-ray diffraction at 3.2Å and 3.3Å resolution, respectively. In d325nTVA II-mβ-CD complex, the orientation and binding-position of β-CD in TVA II were identical to those in cyclodextin glucanotransferase (CGTase). The active site residues were essentialy conserved, while there are no residues corresponding to Tyr89, Phe183, and His233 of CGTase in TVA II. In d325nTVA II-G6 complex, the electron density maps of two glucosyl units at the non-reducing end were disordered and invisible. The four glucosyl units of G6 were bound to TVA II as in CGTase, while the others were not stacked and were probably flexible. The residues of TVA II corresponding to Tyr89, Lys232, and His233 of CGTase were completely lacking. These results suggest that the lack of the residues related to α-glucan and CD-stacking causes the functional distinctions between CGTase and TVA II.</description><subject>a-Amylase II</subject><subject>ALPHA AMYLASE</subject><subject>alpha-Amylases - chemistry</subject><subject>alpha-Amylases - physiology</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>b-Glucan</subject><subject>beta-Cyclodextrins</subject><subject>Biological and medical sciences</subject><subject>CHEMICAL STRUCTURE</subject><subject>crystal structure</subject><subject>Cyclodextrins - chemistry</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glucosyltransferases - chemistry</subject><subject>Hydrolases</subject><subject>methyl ^b-cyclodextrin</subject><subject>Micromonosporaceae - enzymology</subject><subject>Models, Molecular</subject><subject>Oligosaccharides - chemistry</subject><subject>Protein Structure, Tertiary</subject><subject>pullulan</subject><subject>Substrate Specificity</subject><subject>THERMOACTINOMYCES</subject><subject>Thermoactinomyces vulgaris</subject><subject>TVA II</subject><subject>α-amylase</subject><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0U2LFDEQBuAgLu64evGu5CAehB6TTufrKIsfsywoup5DdTqZaUl3xiTtOv_eyMyyHgQhECieqiJvEHpGyZq2kr7p-34t-FpQ_QCtKOtkI3QnH6IV0VQ0quP0HD3O-TshtcDpI3ROKWNESLlC8LWkxZYluYyjxzc7l6YItoxznA62Fn8uYQtpzPhL00kMYb-DBqZDgOzwZoNtnPbB_XIDvh3LDuelzyVBcRhmCHG7uPwEnXkI2T093Rfo2_t3N5cfm-tPHzaXb68b20lZGmuV9tRpRphVzg4WWkZ4PeD5MCjW90ooSSSTHXBLfFefIodeDiC9UtKxC_TqOHef4o-6t5hpzNaFALOLSzaSqFYorv8LqdSk1aqt8PUR2hRzTs6bfRonSAdDifmTvKnJG8FNTb7iF6epSz-54Z6eoq7g5QlAthB8gtmO-S_XasZEZfzIxtnHNMFtTGEwBQ4hprse9s_9z499HqKBbf0xc_W5JYQSwrRu2W9Xfac3</recordid><startdate>20010301</startdate><enddate>20010301</enddate><creator>Yokota, T. (Tokyo Univ. of Agriculture and Technology, Fuchu (Japan))</creator><creator>Tonozuka, T</creator><creator>Shimura, Y</creator><creator>Ichikawa, K</creator><creator>Kamitori, S</creator><creator>Sakano, Y</creator><general>Japan Society for Bioscience, Biotechnology, and Agrochemistry</general><general>Japan Society for Bioscience Biotechnology and Agrochemistry</general><scope>FBQ</scope><scope>IQODW</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20010301</creationdate><title>Structures of Thermoactinomyces vulgaris R-47 alpha-amylase II complexed with substrate analogues</title><author>Yokota, T. (Tokyo Univ. of Agriculture and Technology, Fuchu (Japan)) ; Tonozuka, T ; Shimura, Y ; Ichikawa, K ; Kamitori, S ; Sakano, Y</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c477t-cc89f1e9303c8ecdca2305305af5dd83bb868707374a5c0f49157db7da7f887e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>a-Amylase II</topic><topic>ALPHA AMYLASE</topic><topic>alpha-Amylases - chemistry</topic><topic>alpha-Amylases - physiology</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>b-Glucan</topic><topic>beta-Cyclodextrins</topic><topic>Biological and medical sciences</topic><topic>CHEMICAL STRUCTURE</topic><topic>crystal structure</topic><topic>Cyclodextrins - chemistry</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glucosyltransferases - chemistry</topic><topic>Hydrolases</topic><topic>methyl ^b-cyclodextrin</topic><topic>Micromonosporaceae - enzymology</topic><topic>Models, Molecular</topic><topic>Oligosaccharides - chemistry</topic><topic>Protein Structure, Tertiary</topic><topic>pullulan</topic><topic>Substrate Specificity</topic><topic>THERMOACTINOMYCES</topic><topic>Thermoactinomyces vulgaris</topic><topic>TVA II</topic><topic>α-amylase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yokota, T. (Tokyo Univ. of Agriculture and Technology, Fuchu (Japan))</creatorcontrib><creatorcontrib>Tonozuka, T</creatorcontrib><creatorcontrib>Shimura, Y</creatorcontrib><creatorcontrib>Ichikawa, K</creatorcontrib><creatorcontrib>Kamitori, S</creatorcontrib><creatorcontrib>Sakano, Y</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yokota, T. (Tokyo Univ. of Agriculture and Technology, Fuchu (Japan))</au><au>Tonozuka, T</au><au>Shimura, Y</au><au>Ichikawa, K</au><au>Kamitori, S</au><au>Sakano, Y</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structures of Thermoactinomyces vulgaris R-47 alpha-amylase II complexed with substrate analogues</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>2001-03-01</date><risdate>2001</risdate><volume>65</volume><issue>3</issue><spage>619</spage><epage>626</epage><pages>619-626</pages><issn>0916-8451</issn><eissn>1347-6947</eissn><abstract>The structures of Thermoactinomyces vulgaris R-47 α-amylase II mutant (d325nTVA II) complexed with substrate analogues, methyl β-cyclodextrin (mβ-CD) and maltohexaose (G6), were solved by X-ray diffraction at 3.2Å and 3.3Å resolution, respectively. In d325nTVA II-mβ-CD complex, the orientation and binding-position of β-CD in TVA II were identical to those in cyclodextin glucanotransferase (CGTase). The active site residues were essentialy conserved, while there are no residues corresponding to Tyr89, Phe183, and His233 of CGTase in TVA II. In d325nTVA II-G6 complex, the electron density maps of two glucosyl units at the non-reducing end were disordered and invisible. The four glucosyl units of G6 were bound to TVA II as in CGTase, while the others were not stacked and were probably flexible. The residues of TVA II corresponding to Tyr89, Lys232, and His233 of CGTase were completely lacking. These results suggest that the lack of the residues related to α-glucan and CD-stacking causes the functional distinctions between CGTase and TVA II.</abstract><cop>Tokyo</cop><pub>Japan Society for Bioscience, Biotechnology, and Agrochemistry</pub><pmid>11330677</pmid><doi>10.1271/bbb.65.619</doi><tpages>8</tpages></addata></record> |
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| ispartof | Bioscience, biotechnology, and biochemistry, 2001-03, Vol.65 (3), p.619-626 |
| issn | 0916-8451 1347-6947 |
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| source | J-STAGE Free; MEDLINE; Oxford University Press Journals All Titles (1996-Current); Freely Accessible Japanese Titles; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | a-Amylase II ALPHA AMYLASE alpha-Amylases - chemistry alpha-Amylases - physiology Analytical, structural and metabolic biochemistry b-Glucan beta-Cyclodextrins Biological and medical sciences CHEMICAL STRUCTURE crystal structure Cyclodextrins - chemistry Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Glucosyltransferases - chemistry Hydrolases methyl ^b-cyclodextrin Micromonosporaceae - enzymology Models, Molecular Oligosaccharides - chemistry Protein Structure, Tertiary pullulan Substrate Specificity THERMOACTINOMYCES Thermoactinomyces vulgaris TVA II α-amylase |
| title | Structures of Thermoactinomyces vulgaris R-47 alpha-amylase II complexed with substrate analogues |
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