The structure of E. coli β-galactosidase
E. coli β-galactosidase is a tetramer of four identical 1023-amino acid chains. Each chain consists of five domains, the third of which is an eight-stranded α / β barrel that comprises much of the active site. This site does, however, include elements from other domains and other subunits. The N-ter...
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| Veröffentlicht in: | Comptes rendus. Biologies 2005-06, Vol.328 (6), p.549-556 |
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| container_title | Comptes rendus. Biologies |
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| creator | Matthews, Brian W. |
| description | E. coli β-galactosidase is a tetramer of four identical 1023-amino acid chains. Each chain consists of five domains, the third of which is an eight-stranded
α
/
β
barrel that comprises much of the active site. This site does, however, include elements from other domains and other subunits. The N-terminal region of the polypeptide chains help form one of the subunit interfaces. Taken together these features provide a structural basis for the well-known property of α-complementation. Catalytic activity proceeds via the formation of a covalent galactosyl intermediate with Glu537, and includes ‘shallow’ and ‘deep’ modes of substrate binding.
To cite this article: B.W. Matthews, C. R. Biologies 328 (2005). |
| doi_str_mv | 10.1016/j.crvi.2005.03.006 |
| format | Article |
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α
/
β
barrel that comprises much of the active site. This site does, however, include elements from other domains and other subunits. The N-terminal region of the polypeptide chains help form one of the subunit interfaces. Taken together these features provide a structural basis for the well-known property of α-complementation. Catalytic activity proceeds via the formation of a covalent galactosyl intermediate with Glu537, and includes ‘shallow’ and ‘deep’ modes of substrate binding.
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α
/
β
barrel that comprises much of the active site. This site does, however, include elements from other domains and other subunits. The N-terminal region of the polypeptide chains help form one of the subunit interfaces. Taken together these features provide a structural basis for the well-known property of α-complementation. Catalytic activity proceeds via the formation of a covalent galactosyl intermediate with Glu537, and includes ‘shallow’ and ‘deep’ modes of substrate binding.
To cite this article: B.W. Matthews, C. R. Biologies 328 (2005).</description><subject>Allolactose</subject><subject>beta-Galactosidase - chemistry</subject><subject>Binding Sites</subject><subject>Enzyme Activation</subject><subject>Escherichia coli - enzymology</subject><subject>Hydrogen Bonding</subject><subject>Lactose</subject><subject>Magnesium - metabolism</subject><subject>Models, Molecular</subject><subject>Molecular Structure</subject><subject>Tetramer</subject><subject>α-complementation</subject><subject>β-galactosidase</subject><issn>1631-0691</issn><issn>1768-3238</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMtKxDAUhoMozjj6Ai6kK8FFa9JcC25kGC8w4GZchzQ91Qyd6Zi0A76WD-IzmTIFd7rKyeH7f5IPoUuCM4KJuF1n1u9dlmPMM0wzjMURmhIpVEpzqo7jLChJsSjIBJ2FsMYxVHB-iiaEFzxeyBTdrN4hCZ3vbdd7SNo6WWSJbRuXfH-lb6YxtmuDq0yAc3RSmybAxXjO0OvDYjV_Spcvj8_z-2VqqeJdCgCSMsU4UIZLxmrOKslZXRmhrIRK8HJYCaWMjA8vC6IMqSUYK1hOCNAZuj707nz70UPo9MYFC01jttD2QQtZ5JjGH_4H0lxikgsVwfwAWt-G4KHWO-82xn9qgvVgUq_1YFIPJjWmOpqMoauxvS83UP1GRnURuDsAEGXsHXgdrIOthcp5sJ2uWvdX_w-ZdIM0</recordid><startdate>20050601</startdate><enddate>20050601</enddate><creator>Matthews, Brian W.</creator><general>Elsevier 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>7U5</scope><scope>8FD</scope><scope>L7M</scope><scope>7X8</scope></search><sort><creationdate>20050601</creationdate><title>The structure of E. coli β-galactosidase</title><author>Matthews, Brian W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c385t-eee734845e340b44f54d754fda68c7ed65bf54d688a7005b918a1f7eac64211e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Allolactose</topic><topic>beta-Galactosidase - chemistry</topic><topic>Binding Sites</topic><topic>Enzyme Activation</topic><topic>Escherichia coli - enzymology</topic><topic>Hydrogen Bonding</topic><topic>Lactose</topic><topic>Magnesium - metabolism</topic><topic>Models, Molecular</topic><topic>Molecular Structure</topic><topic>Tetramer</topic><topic>α-complementation</topic><topic>β-galactosidase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Matthews, Brian W.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>MEDLINE - Academic</collection><jtitle>Comptes rendus. Biologies</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Matthews, Brian W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The structure of E. coli β-galactosidase</atitle><jtitle>Comptes rendus. Biologies</jtitle><addtitle>C R Biol</addtitle><date>2005-06-01</date><risdate>2005</risdate><volume>328</volume><issue>6</issue><spage>549</spage><epage>556</epage><pages>549-556</pages><issn>1631-0691</issn><eissn>1768-3238</eissn><abstract>E. coli β-galactosidase is a tetramer of four identical 1023-amino acid chains. Each chain consists of five domains, the third of which is an eight-stranded
α
/
β
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| ispartof | Comptes rendus. Biologies, 2005-06, Vol.328 (6), p.549-556 |
| issn | 1631-0691 1768-3238 |
| language | eng |
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| source | Elsevier ScienceDirect Journals Complete - AutoHoldings; MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Allolactose beta-Galactosidase - chemistry Binding Sites Enzyme Activation Escherichia coli - enzymology Hydrogen Bonding Lactose Magnesium - metabolism Models, Molecular Molecular Structure Tetramer α-complementation β-galactosidase |
| title | The structure of E. coli β-galactosidase |
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