Metal-ion induced conformational changes in alkaline phosphatase from E. coli assessed by limited proteolysis
Alkaline phosphatase (AP) displays significant structural changes during metal-ion binding, supporting cooperative interactions between the subunits of the dimeric enzyme. Here, we present data on the dynamic properties of AP from E. coli, and characterize the structural changes that accompany varia...
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| Veröffentlicht in: | Biochimie 2004-06, Vol.86 (6), p.403-409 |
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| creator | Bučević-Popović, V. Pavela-Vrančič, M. Dieckmann, R. |
| description | Alkaline phosphatase (AP) displays significant structural changes during metal-ion binding, supporting cooperative interactions between the subunits of the dimeric enzyme. Here, we present data on the dynamic properties of AP from
E. coli, and characterize the structural changes that accompany variations in metal-ion content, combining limited proteolysis and MALDI-TOF mass spectrometry. Limited proteolysis revealed an internal cleavage site at Arg-293, reflecting a position of conformational flexibility supporting subunit communication essential for catalysis. A specific shielding of a region distant from the metal-binding site has been demonstrated, implying transmission of conformational changes, induced by metal-ion binding to the adjacent subunit, across the subunit interface. |
| doi_str_mv | 10.1016/j.biochi.2004.05.001 |
| format | Article |
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E. coli, and characterize the structural changes that accompany variations in metal-ion content, combining limited proteolysis and MALDI-TOF mass spectrometry. Limited proteolysis revealed an internal cleavage site at Arg-293, reflecting a position of conformational flexibility supporting subunit communication essential for catalysis. A specific shielding of a region distant from the metal-binding site has been demonstrated, implying transmission of conformational changes, induced by metal-ion binding to the adjacent subunit, across the subunit interface.</description><subject>Alkaline phosphatase</subject><subject>Alkaline Phosphatase - chemistry</subject><subject>Alkaline Phosphatase - drug effects</subject><subject>Alkaline Phosphatase - metabolism</subject><subject>Binding Sites</subject><subject>Conformational change</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Escherichia coli Proteins - drug effects</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Ions - metabolism</subject><subject>Ions - pharmacology</subject><subject>Limited proteolysis</subject><subject>Magnesium - metabolism</subject><subject>Magnesium - pharmacology</subject><subject>MALDI-TOF mass spectrometry</subject><subject>Metal ion</subject><subject>Metals - metabolism</subject><subject>Metals - pharmacology</subject><subject>Protein Conformation</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods</subject><subject>Trypsin - metabolism</subject><subject>Zinc - metabolism</subject><subject>Zinc - pharmacology</subject><issn>0300-9084</issn><issn>1638-6183</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtLLDEQhYNc0fHxD-SSlbtuK53HZDaCiC9Q3Og6pNPVTuamO2PSI8y_NzID7i4EEirnnKr6CLlgUDNg6mpVtz66pa8bAFGDrAHYAZkxxXWlmOZ_yAw4QLUALY7JSc4rAJDQLI7IMZNcapDzGRlecLKh8nGkfuw2Djvq4tjHNNipFG2gbmnHD8zlm9rwzwY_Il0vY14v7WQz0j7Fgd7VxRY8tTljOR1ttzT4wU_luU5xwhi22eczctjbkPF8f5-S9_u7t9vH6vn14en25rlyZa6pkrLFHh0TqLtWC7GwqBX2TjBUCiyfo5pLhrxzre6bUhWSOa7axgrBeNvzU3K5yy29PzeYJzP47DAEO2LcZKOUVrBoZBGKndClmHPC3qyTH2zaGgbmB7NZmR1m84PZgDQFc7H93edv2gG7X9OeaxFc7wRYtvzymEx2HseC1yd0k-mi_3-Hb3f0kkA</recordid><startdate>20040601</startdate><enddate>20040601</enddate><creator>Bučević-Popović, V.</creator><creator>Pavela-Vrančič, M.</creator><creator>Dieckmann, R.</creator><general>Elsevier Masson SAS</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>7X8</scope></search><sort><creationdate>20040601</creationdate><title>Metal-ion induced conformational changes in alkaline phosphatase from E. coli assessed by limited proteolysis</title><author>Bučević-Popović, V. ; 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Here, we present data on the dynamic properties of AP from
E. coli, and characterize the structural changes that accompany variations in metal-ion content, combining limited proteolysis and MALDI-TOF mass spectrometry. Limited proteolysis revealed an internal cleavage site at Arg-293, reflecting a position of conformational flexibility supporting subunit communication essential for catalysis. A specific shielding of a region distant from the metal-binding site has been demonstrated, implying transmission of conformational changes, induced by metal-ion binding to the adjacent subunit, across the subunit interface.</abstract><cop>France</cop><pub>Elsevier Masson SAS</pub><pmid>15358057</pmid><doi>10.1016/j.biochi.2004.05.001</doi><tpages>7</tpages></addata></record> |
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| identifier | ISSN: 0300-9084 |
| ispartof | Biochimie, 2004-06, Vol.86 (6), p.403-409 |
| issn | 0300-9084 1638-6183 |
| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Alkaline phosphatase Alkaline Phosphatase - chemistry Alkaline Phosphatase - drug effects Alkaline Phosphatase - metabolism Binding Sites Conformational change Escherichia coli Proteins - chemistry Escherichia coli Proteins - drug effects Escherichia coli Proteins - metabolism Ions - metabolism Ions - pharmacology Limited proteolysis Magnesium - metabolism Magnesium - pharmacology MALDI-TOF mass spectrometry Metal ion Metals - metabolism Metals - pharmacology Protein Conformation Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods Trypsin - metabolism Zinc - metabolism Zinc - pharmacology |
| title | Metal-ion induced conformational changes in alkaline phosphatase from E. coli assessed by limited proteolysis |
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