Tandem Repeat of a Seven-Bladed β-Propeller Domain in Oligoxyloglucan Reducing-End-Specific Cellobiohydrolase
Oligoxyloglucan reducing-end-specific cellobiohydrolase (OXG-RCBH; EC 3.2.1.150) is an exoglucanase that recognizes the reducing end of oligoxyloglucan and releases two glucosyl residue segments from the main chain. The X-ray crystal structure of OXG-RCBH determined at 2.2 Å resolution reveals a uni...
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| Veröffentlicht in: | Structure (London) 2004-07, Vol.12 (7), p.1209-1217 |
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| creator | Yaoi, Katsuro Kondo, Hidemasa Noro, Natsuko Suzuki, Mamoru Tsuda, Sakae Mitsuishi, Yasushi |
| description | Oligoxyloglucan reducing-end-specific cellobiohydrolase (OXG-RCBH; EC 3.2.1.150) is an exoglucanase that recognizes the reducing end of oligoxyloglucan and releases two glucosyl residue segments from the main chain. The X-ray crystal structure of OXG-RCBH determined at 2.2 Å resolution reveals a unique feature of this enzyme; OXG-RCBH consists of a tandem repeat of two similar domains, which are both folded into seven-bladed β-propeller structures. The sequence alignment of the propeller blades, based on the structure, indicates that a weak repeat of the amino acid sequence occurred seven times to construct each domain. There is a cleft that can accommodate the substrate oligosaccharide between the two domains, which is a putative substrate binding subsite. Mutation of either Asp35 or Asp465, located in the putative catalytic center, to Asn resulted in a protein with no detectable catalytic activity, indicating the critical role of these amino acids in catalysis. |
| doi_str_mv | 10.1016/j.str.2004.04.020 |
| format | Article |
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The X-ray crystal structure of OXG-RCBH determined at 2.2 Å resolution reveals a unique feature of this enzyme; OXG-RCBH consists of a tandem repeat of two similar domains, which are both folded into seven-bladed β-propeller structures. The sequence alignment of the propeller blades, based on the structure, indicates that a weak repeat of the amino acid sequence occurred seven times to construct each domain. There is a cleft that can accommodate the substrate oligosaccharide between the two domains, which is a putative substrate binding subsite. Mutation of either Asp35 or Asp465, located in the putative catalytic center, to Asn resulted in a protein with no detectable catalytic activity, indicating the critical role of these amino acids in catalysis.</description><identifier>ISSN: 0969-2126</identifier><identifier>EISSN: 1878-4186</identifier><identifier>DOI: 10.1016/j.str.2004.04.020</identifier><identifier>PMID: 15242597</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Cellulose 1,4-beta-Cellobiosidase - chemistry ; Cellulose 1,4-beta-Cellobiosidase - metabolism ; Crystallography, X-Ray ; Models, Molecular ; Molecular Sequence Data ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Tandem Repeat Sequences</subject><ispartof>Structure (London), 2004-07, Vol.12 (7), p.1209-1217</ispartof><rights>2004 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c392t-565e8f8783e4b4f58a3398f21cff4143cecc80d034f71263d99488c5be85463a3</citedby><cites>FETCH-LOGICAL-c392t-565e8f8783e4b4f58a3398f21cff4143cecc80d034f71263d99488c5be85463a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.str.2004.04.020$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15242597$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yaoi, Katsuro</creatorcontrib><creatorcontrib>Kondo, Hidemasa</creatorcontrib><creatorcontrib>Noro, Natsuko</creatorcontrib><creatorcontrib>Suzuki, Mamoru</creatorcontrib><creatorcontrib>Tsuda, Sakae</creatorcontrib><creatorcontrib>Mitsuishi, Yasushi</creatorcontrib><title>Tandem Repeat of a Seven-Bladed β-Propeller Domain in Oligoxyloglucan Reducing-End-Specific Cellobiohydrolase</title><title>Structure (London)</title><addtitle>Structure</addtitle><description>Oligoxyloglucan reducing-end-specific cellobiohydrolase (OXG-RCBH; EC 3.2.1.150) is an exoglucanase that recognizes the reducing end of oligoxyloglucan and releases two glucosyl residue segments from the main chain. The X-ray crystal structure of OXG-RCBH determined at 2.2 Å resolution reveals a unique feature of this enzyme; OXG-RCBH consists of a tandem repeat of two similar domains, which are both folded into seven-bladed β-propeller structures. The sequence alignment of the propeller blades, based on the structure, indicates that a weak repeat of the amino acid sequence occurred seven times to construct each domain. There is a cleft that can accommodate the substrate oligosaccharide between the two domains, which is a putative substrate binding subsite. Mutation of either Asp35 or Asp465, located in the putative catalytic center, to Asn resulted in a protein with no detectable catalytic activity, indicating the critical role of these amino acids in catalysis.</description><subject>Amino Acid Sequence</subject><subject>Cellulose 1,4-beta-Cellobiosidase - chemistry</subject><subject>Cellulose 1,4-beta-Cellobiosidase - metabolism</subject><subject>Crystallography, X-Ray</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Protein Folding</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>Tandem Repeat Sequences</subject><issn>0969-2126</issn><issn>1878-4186</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM1uEzEUhS0EomnLA7BBs2Ln4P94xApCW5AqFbVlbTn2dXA0Mx7smYq8Fg_SZ8JRIrFDOtLdnO_onoPQW0qWlFD1YbcsU14yQsTyIEZeoAXVK40F1eolWpBWtZhRps7QeSk7QgiThLxGZ1QywWS7WqDh0Q4e-uYeRrBTk0Jjmwd4ggF_7qwH3zz_wd9zGqHrIDdfUm_j0FTddXGbfu-7tO1mZ4fK-9nFYYuvBo8fRnAxRNesK5Y2Mf3c-5w6W-ASvQq2K_DmdC_Qj-urx_VXfHt382396RY73rIJSyVBh9qEg9iIILXlvNWBUReCoII7cE4TT7gIq1qP-7YVWju5AS2F4pZfoPfH3DGnXzOUyfSxuPqNHSDNxSilWkqkqEZ6NLqcSskQzJhjb_PeUGIOI5udqSObw8jmIEYq8-4UPm968P-I06rV8PFogFrxKUI2xUUYHPiYwU3Gp_if-L9J6o4g</recordid><startdate>20040701</startdate><enddate>20040701</enddate><creator>Yaoi, Katsuro</creator><creator>Kondo, Hidemasa</creator><creator>Noro, Natsuko</creator><creator>Suzuki, Mamoru</creator><creator>Tsuda, Sakae</creator><creator>Mitsuishi, Yasushi</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>20040701</creationdate><title>Tandem Repeat of a Seven-Bladed β-Propeller Domain in Oligoxyloglucan Reducing-End-Specific Cellobiohydrolase</title><author>Yaoi, Katsuro ; Kondo, Hidemasa ; Noro, Natsuko ; Suzuki, Mamoru ; Tsuda, Sakae ; Mitsuishi, Yasushi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c392t-565e8f8783e4b4f58a3398f21cff4143cecc80d034f71263d99488c5be85463a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amino Acid Sequence</topic><topic>Cellulose 1,4-beta-Cellobiosidase - chemistry</topic><topic>Cellulose 1,4-beta-Cellobiosidase - metabolism</topic><topic>Crystallography, X-Ray</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Protein Folding</topic><topic>Protein Structure, Secondary</topic><topic>Protein Structure, Tertiary</topic><topic>Tandem Repeat Sequences</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yaoi, Katsuro</creatorcontrib><creatorcontrib>Kondo, Hidemasa</creatorcontrib><creatorcontrib>Noro, Natsuko</creatorcontrib><creatorcontrib>Suzuki, Mamoru</creatorcontrib><creatorcontrib>Tsuda, Sakae</creatorcontrib><creatorcontrib>Mitsuishi, Yasushi</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>Yaoi, Katsuro</au><au>Kondo, Hidemasa</au><au>Noro, Natsuko</au><au>Suzuki, Mamoru</au><au>Tsuda, Sakae</au><au>Mitsuishi, Yasushi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tandem Repeat of a Seven-Bladed β-Propeller Domain in Oligoxyloglucan Reducing-End-Specific Cellobiohydrolase</atitle><jtitle>Structure (London)</jtitle><addtitle>Structure</addtitle><date>2004-07-01</date><risdate>2004</risdate><volume>12</volume><issue>7</issue><spage>1209</spage><epage>1217</epage><pages>1209-1217</pages><issn>0969-2126</issn><eissn>1878-4186</eissn><abstract>Oligoxyloglucan reducing-end-specific cellobiohydrolase (OXG-RCBH; EC 3.2.1.150) is an exoglucanase that recognizes the reducing end of oligoxyloglucan and releases two glucosyl residue segments from the main chain. 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| source | MEDLINE; Cell Press Free Archives; ScienceDirect Journals (5 years ago - present); EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Cellulose 1,4-beta-Cellobiosidase - chemistry Cellulose 1,4-beta-Cellobiosidase - metabolism Crystallography, X-Ray Models, Molecular Molecular Sequence Data Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Tandem Repeat Sequences |
| title | Tandem Repeat of a Seven-Bladed β-Propeller Domain in Oligoxyloglucan Reducing-End-Specific Cellobiohydrolase |
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