A novel calcium binding site in the galactose-binding protein of bacterial transport and chemotaxis
The refined 1.9-A resolution structure of the periplasmic D-galactose-binding protein (GBP) reveals a calcium ion surrounded by seven ligands, all protein oxygen atoms. A nine-residue loop (amino-acid positions 134-142), which is preceded by a beta-turn and followed by a beta-strand, provides five l...
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| Veröffentlicht in: | Nature (London) 1987-06, Vol.327 (6123), p.635-638 |
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| creator | Vyas, Nand K Vyas, Meenakshi N Quiocho, Florante A |
| description | The refined 1.9-A resolution structure of the periplasmic D-galactose-binding protein (GBP) reveals a calcium ion surrounded by seven ligands, all protein oxygen atoms. A nine-residue loop (amino-acid positions 134-142), which is preceded by a beta-turn and followed by a beta-strand, provides five ligands from every second residue. The last two ligands are supplied by the carboxylate group of Glu 205. The entire GBP Ca2+-binding site adopts a conformation very similar to the site in the 'helix-loop-helix' or 'EF-hand' unit commonly found in intracellular calcium-binding proteins, but without the two helices. Structural analyses have also uncovered the sugar-binding site some 30 A from the calcium and a site for interacting with the membrane-bound trg chemotactic signal transducer approximately 45 A from the calcium. Our results show that a common tight calcium binding site of ancient origin can be tethered to different secondary structures. They also provide the first demonstration of a metal-binding site in a protein which is involved in bacterial active transport and chemotaxis. |
| doi_str_mv | 10.1038/327635a0 |
| format | Article |
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A nine-residue loop (amino-acid positions 134-142), which is preceded by a beta-turn and followed by a beta-strand, provides five ligands from every second residue. The last two ligands are supplied by the carboxylate group of Glu 205. The entire GBP Ca2+-binding site adopts a conformation very similar to the site in the 'helix-loop-helix' or 'EF-hand' unit commonly found in intracellular calcium-binding proteins, but without the two helices. Structural analyses have also uncovered the sugar-binding site some 30 A from the calcium and a site for interacting with the membrane-bound trg chemotactic signal transducer approximately 45 A from the calcium. Our results show that a common tight calcium binding site of ancient origin can be tethered to different secondary structures. They also provide the first demonstration of a metal-binding site in a protein which is involved in bacterial active transport and chemotaxis.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/327635a0</identifier><identifier>PMID: 3600760</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing</publisher><subject>Amino Acid Sequence ; Bacteria ; Bacterial Physiological Phenomena ; Binding Sites ; Biological and medical sciences ; Biological Transport ; Calcium ; Calcium - metabolism ; Calcium-Binding Proteins ; Carrier Proteins - metabolism ; Chemistry ; Chemotaxis ; Fundamental and applied biological sciences. Psychology ; Galactose - metabolism ; galactose-binding protein ; Medical research ; Models, Molecular ; Molecular biophysics ; Monosaccharide Transport Proteins ; Periplasmic Binding Proteins ; Protein Binding ; Protein Conformation ; Proteins ; Structure in molecular biology ; Tridimensional structure ; X-ray crystallography ; X-Ray Diffraction</subject><ispartof>Nature (London), 1987-06, Vol.327 (6123), p.635-638</ispartof><rights>1987 INIST-CNRS</rights><rights>Copyright Macmillan Journals Ltd. Jun 18, 1987</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c516t-95af19830e8a7464d972c01b6d9ceb92c1193f1c3d39140c1cfb78e7ed1236883</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,27929,27930</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8333914$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3600760$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vyas, Nand K</creatorcontrib><creatorcontrib>Vyas, Meenakshi N</creatorcontrib><creatorcontrib>Quiocho, Florante A</creatorcontrib><title>A novel calcium binding site in the galactose-binding protein of bacterial transport and chemotaxis</title><title>Nature (London)</title><addtitle>Nature</addtitle><description>The refined 1.9-A resolution structure of the periplasmic D-galactose-binding protein (GBP) reveals a calcium ion surrounded by seven ligands, all protein oxygen atoms. A nine-residue loop (amino-acid positions 134-142), which is preceded by a beta-turn and followed by a beta-strand, provides five ligands from every second residue. The last two ligands are supplied by the carboxylate group of Glu 205. The entire GBP Ca2+-binding site adopts a conformation very similar to the site in the 'helix-loop-helix' or 'EF-hand' unit commonly found in intracellular calcium-binding proteins, but without the two helices. Structural analyses have also uncovered the sugar-binding site some 30 A from the calcium and a site for interacting with the membrane-bound trg chemotactic signal transducer approximately 45 A from the calcium. Our results show that a common tight calcium binding site of ancient origin can be tethered to different secondary structures. They also provide the first demonstration of a metal-binding site in a protein which is involved in bacterial active transport and chemotaxis.</description><subject>Amino Acid Sequence</subject><subject>Bacteria</subject><subject>Bacterial Physiological Phenomena</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Biological Transport</subject><subject>Calcium</subject><subject>Calcium - metabolism</subject><subject>Calcium-Binding Proteins</subject><subject>Carrier Proteins - metabolism</subject><subject>Chemistry</subject><subject>Chemotaxis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Galactose - metabolism</subject><subject>galactose-binding protein</subject><subject>Medical research</subject><subject>Models, Molecular</subject><subject>Molecular biophysics</subject><subject>Monosaccharide Transport Proteins</subject><subject>Periplasmic Binding Proteins</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Proteins</subject><subject>Structure in molecular biology</subject><subject>Tridimensional structure</subject><subject>X-ray crystallography</subject><subject>X-Ray Diffraction</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU2LFDEQhoMo6zgK_gEliIiX1qoknaSPy-IXLHjRc5NOp3ezdCdjkl7035thZlbwMqcc3oe3KvUQ8hLhAwLXHzlTkrcGHpENCiUbIbV6TDYATDeguXxKnuV8BwAtKnFBLrgEUBI2xF7SEO_dTK2ZrV8XOvgw-nBDsy-O-kDLraM3Zja2xOyaU7pLsbiaxokONXLJm5mWZELexVSoCSO1t26Jxfz2-Tl5Mpk5uxfHd0t-fv704-prc_39y7ery-vGtihL07Vmwk5zcNooIcXYKWYBBzl21g0ds4gdn9DykXcowKKdBqWdciMyLrXmW_Lu0Fu3-7W6XPrFZ-vm2QQX19yr-mNVD3MW5LJlUojuLMgQFQfFzoJ7KahwP_rNf-BdXFOoZ-kZCIGaV59b8v4A2RRzTm7qd8kvJv3pEfq97_7ku6Kvjn3rsLjxATwKrvnbY25yVTxVRdbnB0xzvj9mxV4fsGDKmty_mtOcvwY5ufo</recordid><startdate>19870618</startdate><enddate>19870618</enddate><creator>Vyas, Nand K</creator><creator>Vyas, Meenakshi N</creator><creator>Quiocho, Florante A</creator><general>Nature Publishing</general><general>Nature Publishing Group</general><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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7ST</scope><scope>7T5</scope><scope>7TG</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>K9.</scope><scope>KL.</scope><scope>M7N</scope><scope>NAPCQ</scope><scope>P64</scope><scope>RC3</scope><scope>SOI</scope><scope>7SC</scope><scope>7SP</scope><scope>7SR</scope><scope>7TB</scope><scope>7U5</scope><scope>8BQ</scope><scope>F28</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>7X8</scope></search><sort><creationdate>19870618</creationdate><title>A novel calcium binding site in the galactose-binding protein of bacterial transport and chemotaxis</title><author>Vyas, Nand K ; Vyas, Meenakshi N ; Quiocho, Florante A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c516t-95af19830e8a7464d972c01b6d9ceb92c1193f1c3d39140c1cfb78e7ed1236883</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Amino Acid Sequence</topic><topic>Bacteria</topic><topic>Bacterial Physiological Phenomena</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Biological Transport</topic><topic>Calcium</topic><topic>Calcium - metabolism</topic><topic>Calcium-Binding Proteins</topic><topic>Carrier Proteins - metabolism</topic><topic>Chemistry</topic><topic>Chemotaxis</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Galactose - metabolism</topic><topic>galactose-binding protein</topic><topic>Medical research</topic><topic>Models, Molecular</topic><topic>Molecular biophysics</topic><topic>Monosaccharide Transport Proteins</topic><topic>Periplasmic Binding Proteins</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Proteins</topic><topic>Structure in molecular biology</topic><topic>Tridimensional structure</topic><topic>X-ray crystallography</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vyas, Nand K</creatorcontrib><creatorcontrib>Vyas, Meenakshi N</creatorcontrib><creatorcontrib>Quiocho, Florante A</creatorcontrib><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>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Environment Abstracts</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Meteorological & Geoastrophysical Abstracts - Academic</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Nursing & Allied Health Premium</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>MEDLINE - Academic</collection><jtitle>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vyas, Nand K</au><au>Vyas, Meenakshi N</au><au>Quiocho, Florante A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel calcium binding site in the galactose-binding protein of bacterial transport and chemotaxis</atitle><jtitle>Nature (London)</jtitle><addtitle>Nature</addtitle><date>1987-06-18</date><risdate>1987</risdate><volume>327</volume><issue>6123</issue><spage>635</spage><epage>638</epage><pages>635-638</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>The refined 1.9-A resolution structure of the periplasmic D-galactose-binding protein (GBP) reveals a calcium ion surrounded by seven ligands, all protein oxygen atoms. 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They also provide the first demonstration of a metal-binding site in a protein which is involved in bacterial active transport and chemotaxis.</abstract><cop>London</cop><pub>Nature Publishing</pub><pmid>3600760</pmid><doi>10.1038/327635a0</doi><tpages>4</tpages></addata></record> |
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| subjects | Amino Acid Sequence Bacteria Bacterial Physiological Phenomena Binding Sites Biological and medical sciences Biological Transport Calcium Calcium - metabolism Calcium-Binding Proteins Carrier Proteins - metabolism Chemistry Chemotaxis Fundamental and applied biological sciences. Psychology Galactose - metabolism galactose-binding protein Medical research Models, Molecular Molecular biophysics Monosaccharide Transport Proteins Periplasmic Binding Proteins Protein Binding Protein Conformation Proteins Structure in molecular biology Tridimensional structure X-ray crystallography X-Ray Diffraction |
| title | A novel calcium binding site in the galactose-binding protein of bacterial transport and chemotaxis |
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