The Crystal Structure of a Multifunctional Protein: Phosphoglucose Isomerase/Autocrine Motility Factor/Neuroleukin
Phosphoglucose isomerase (PGI) plays a central role in both the glycolysis and the gluconeogenesis pathways. We present here the complete crystal structure of PGI from Bacillus stearothermophilus at 2.3- angstrom resolution. We show that PGI has cell-motility-stimulating activity on mouse colon canc...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1999-05, Vol.96 (10), p.5412-5417 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Sun, Yuh-Ju Chou, Chia-Cheng Chen, Wei-Shone Wu, Rong-Tsun Meng, Menghsiao Hsiao, Chwan-Deng |
| description | Phosphoglucose isomerase (PGI) plays a central role in both the glycolysis and the gluconeogenesis pathways. We present here the complete crystal structure of PGI from Bacillus stearothermophilus at 2.3- angstrom resolution. We show that PGI has cell-motility-stimulating activity on mouse colon cancer cells similar to that of endogenous autocrine motility factor (AMF). PGI can also enhance neurite outgrowth on neuronal progenitor cells similar to that observed for neuroleukin. The results confirm that PGI is neuroleukin and AMF. PGI has an open twisted α /β structural motif consisting of two globular domains and two protruding parts. Based on this substrate-free structure, together with the previously published biological, biochemical, and modeling results, we postulate a possible substrate-binding site that is located within the domains' interface for PGI and AMF. In addition, the structure provides evidence suggesting that the top part of the large domain together with one of the protruding loops might participate in inducing the neurotrophic activity. |
| doi_str_mv | 10.1073/pnas.96.10.5412 |
| format | Article |
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We present here the complete crystal structure of PGI from Bacillus stearothermophilus at 2.3- angstrom resolution. We show that PGI has cell-motility-stimulating activity on mouse colon cancer cells similar to that of endogenous autocrine motility factor (AMF). PGI can also enhance neurite outgrowth on neuronal progenitor cells similar to that observed for neuroleukin. The results confirm that PGI is neuroleukin and AMF. PGI has an open twisted α /β structural motif consisting of two globular domains and two protruding parts. Based on this substrate-free structure, together with the previously published biological, biochemical, and modeling results, we postulate a possible substrate-binding site that is located within the domains' interface for PGI and AMF. In addition, the structure provides evidence suggesting that the top part of the large domain together with one of the protruding loops might participate in inducing the neurotrophic activity.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.96.10.5412</identifier><identifier>PMID: 10318897</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Amino Acid Sequence ; Amino acids ; Animals ; Atoms ; Bacillus stearothermophilus ; Binding Sites ; Biochemistry ; Biological Sciences ; Cell motility ; Colon cancer ; Crystal structure ; Crystallography ; Crystallography, X-Ray ; Dimers ; Enzymes ; Epidermal Growth Factor - pharmacology ; Geobacillus stearothermophilus ; Glucose-6-Phosphate Isomerase - chemistry ; Mice ; Models, Molecular ; Molecular Sequence Data ; Molecules ; Neurites ; Neurons ; Phosphates ; Protein Structure, Secondary ; Proteins ; Rats ; Rats, Sprague-Dawley ; Sequence Alignment ; Static Electricity ; Tumor Cells, Cultured</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1999-05, Vol.96 (10), p.5412-5417</ispartof><rights>Copyright 1993-1999 The National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences May 11, 1999</rights><rights>Copyright © 1999, The National Academy of Sciences 1999</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c585t-98196c8b5512b32055c74640af3393f294d2117e78d8c8f008af8a808fa58f13</citedby><cites>FETCH-LOGICAL-c585t-98196c8b5512b32055c74640af3393f294d2117e78d8c8f008af8a808fa58f13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/96/10.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/48130$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/48130$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,315,728,781,785,804,886,27928,27929,53795,53797,58021,58254</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10318897$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sun, Yuh-Ju</creatorcontrib><creatorcontrib>Chou, Chia-Cheng</creatorcontrib><creatorcontrib>Chen, Wei-Shone</creatorcontrib><creatorcontrib>Wu, Rong-Tsun</creatorcontrib><creatorcontrib>Meng, Menghsiao</creatorcontrib><creatorcontrib>Hsiao, Chwan-Deng</creatorcontrib><title>The Crystal Structure of a Multifunctional Protein: Phosphoglucose Isomerase/Autocrine Motility Factor/Neuroleukin</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Phosphoglucose isomerase (PGI) plays a central role in both the glycolysis and the gluconeogenesis pathways. We present here the complete crystal structure of PGI from Bacillus stearothermophilus at 2.3- angstrom resolution. We show that PGI has cell-motility-stimulating activity on mouse colon cancer cells similar to that of endogenous autocrine motility factor (AMF). PGI can also enhance neurite outgrowth on neuronal progenitor cells similar to that observed for neuroleukin. The results confirm that PGI is neuroleukin and AMF. PGI has an open twisted α /β structural motif consisting of two globular domains and two protruding parts. Based on this substrate-free structure, together with the previously published biological, biochemical, and modeling results, we postulate a possible substrate-binding site that is located within the domains' interface for PGI and AMF. In addition, the structure provides evidence suggesting that the top part of the large domain together with one of the protruding loops might participate in inducing the neurotrophic activity.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Atoms</subject><subject>Bacillus stearothermophilus</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biological Sciences</subject><subject>Cell motility</subject><subject>Colon cancer</subject><subject>Crystal structure</subject><subject>Crystallography</subject><subject>Crystallography, X-Ray</subject><subject>Dimers</subject><subject>Enzymes</subject><subject>Epidermal Growth Factor - pharmacology</subject><subject>Geobacillus stearothermophilus</subject><subject>Glucose-6-Phosphate Isomerase - chemistry</subject><subject>Mice</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Molecules</subject><subject>Neurites</subject><subject>Neurons</subject><subject>Phosphates</subject><subject>Protein Structure, Secondary</subject><subject>Proteins</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>Sequence Alignment</subject><subject>Static Electricity</subject><subject>Tumor Cells, Cultured</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1vEzEQxS0EomnhjMQBrTiU0yb-XNuISxVRqNRCJXK3HMduHJx18Aci_z27SqlSDnAajd7vjWbmAfAKwSmCnMx2vc5T2Q3NlFGEn4AJghK1HZXwKZhAiHkrKKYn4DTnDYRQMgGfgxMECRJC8glIi7Vt5mmfiw7Nt5KqKTXZJrpGNzc1FO9qb4qP_SDfplis7983t-uYd-t4F6qJ2TZXOW5t0tnOLmqJJvneNjex-ODLvrnUpsQ0-2JrisHW775_AZ45HbJ9eV_PwOLy42L-ub3--ulqfnHdGiZYaaVAsjNiyRjCS4IhY4bTjkLtCJHEYUlXGCFuuVgJIxyEQjuhBRROM-EQOQMfDmN3dbm1K2P7knRQu-S3Ou1V1F49Vnq_Vnfxp8JIcDLYz-_tKf6oNhe19dnYEHRvY82qk5xRMjzyfyDiWELO-AC-_QvcxJqGx2aFISK0w2KEZgfIpJhzsu5hYQTVGLkaI1eyG_sx8sHx5vjOI_6Q8REwOv_Ijya8-yegXA2h2F9lIF8fyE0eQn1AqUAEkt-pI8qj</recordid><startdate>19990511</startdate><enddate>19990511</enddate><creator>Sun, Yuh-Ju</creator><creator>Chou, Chia-Cheng</creator><creator>Chen, Wei-Shone</creator><creator>Wu, Rong-Tsun</creator><creator>Meng, Menghsiao</creator><creator>Hsiao, Chwan-Deng</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>National Academy of Sciences</general><general>The National Academy of Sciences</general><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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19990511</creationdate><title>The Crystal Structure of a Multifunctional Protein: Phosphoglucose Isomerase/Autocrine Motility Factor/Neuroleukin</title><author>Sun, Yuh-Ju ; 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We present here the complete crystal structure of PGI from Bacillus stearothermophilus at 2.3- angstrom resolution. We show that PGI has cell-motility-stimulating activity on mouse colon cancer cells similar to that of endogenous autocrine motility factor (AMF). PGI can also enhance neurite outgrowth on neuronal progenitor cells similar to that observed for neuroleukin. The results confirm that PGI is neuroleukin and AMF. PGI has an open twisted α /β structural motif consisting of two globular domains and two protruding parts. Based on this substrate-free structure, together with the previously published biological, biochemical, and modeling results, we postulate a possible substrate-binding site that is located within the domains' interface for PGI and AMF. In addition, the structure provides evidence suggesting that the top part of the large domain together with one of the protruding loops might participate in inducing the neurotrophic activity.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>10318897</pmid><doi>10.1073/pnas.96.10.5412</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Amino acids Animals Atoms Bacillus stearothermophilus Binding Sites Biochemistry Biological Sciences Cell motility Colon cancer Crystal structure Crystallography Crystallography, X-Ray Dimers Enzymes Epidermal Growth Factor - pharmacology Geobacillus stearothermophilus Glucose-6-Phosphate Isomerase - chemistry Mice Models, Molecular Molecular Sequence Data Molecules Neurites Neurons Phosphates Protein Structure, Secondary Proteins Rats Rats, Sprague-Dawley Sequence Alignment Static Electricity Tumor Cells, Cultured |
| title | The Crystal Structure of a Multifunctional Protein: Phosphoglucose Isomerase/Autocrine Motility Factor/Neuroleukin |
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