Nucleotide Control of Interdomain Interactions in the Conformational Reaction Cycle of SecA
The SecA adenosine triphosphatase (ATPase) mediates extrusion of the amino termini of secreted proteins from the eubacterial cytosol based on cycles of reversible binding to the SecYEG translocon. We have determined the crystal structure of SecA with and without magnesium-adenosine diphosphate bound...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2002-09, Vol.297 (5589), p.2018-2026 |
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| container_title | Science (American Association for the Advancement of Science) |
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| creator | Hunt, John F. Weinkauf, Sevil Henry, Lisa Fak, John J. McNicholas, Paul Oliver, Donald B. Deisenhofer, Johann |
| description | The SecA adenosine triphosphatase (ATPase) mediates extrusion of the amino termini of secreted proteins from the eubacterial cytosol based on cycles of reversible binding to the SecYEG translocon. We have determined the crystal structure of SecA with and without magnesium-adenosine diphosphate bound to the high-affinity ATPase site at 3.0 and 2.7 angstrom resolution, respectively. Candidate sites for preprotein binding are located on a surface containing the SecA epitopes exposed to the periplasm upon binding to SecYEG and are thus positioned to deliver preprotein to SecYEG. Comparisons with structurally related ATPases, including superfamily I and II ATP-dependent helicases, suggest that the interaction geometry of the tandem motor domains in SecA is modulated by nucleotide binding, which is shown by fluorescence anisotropy experiments to reverse an endothermic domain-dissociation reaction hypothesized to gate binding to SecYEG. |
| doi_str_mv | 10.1126/science.1074424 |
| format | Article |
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Comparisons with structurally related ATPases, including superfamily I and II ATP-dependent helicases, suggest that the interaction geometry of the tandem motor domains in SecA is modulated by nucleotide binding, which is shown by fluorescence anisotropy experiments to reverse an endothermic domain-dissociation reaction hypothesized to gate binding to SecYEG.</description><identifier>ISSN: 0036-8075</identifier><identifier>ISSN: 0193-4511</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.1074424</identifier><identifier>PMID: 12242434</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Association for the Advancement of Science</publisher><subject>Adenosine Diphosphate - chemistry ; Adenosine Diphosphate - metabolism ; Adenosine triphosphatase ; Adenosine triphosphatases ; Adenosine Triphosphatases - chemistry ; Adenosine Triphosphatases - metabolism ; Adenosine Triphosphate - chemistry ; Adenosine Triphosphate - metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Anisotropy ; ATPases ; Bacillus subtilis - enzymology ; Bacteria ; Bacterial Proteins - chemistry ; Bacterial Proteins - metabolism ; Base sequence ; BASIC BIOLOGICAL SCIENCES ; Binding Sites ; Biochemistry ; Biological and medical sciences ; BIOLOGICAL FUNCTIONS ; Crystal structure ; Crystalline structure ; Crystallization ; Crystallography ; Crystallography, X-Ray ; Dimerization ; Dimers ; DNA Helicases - chemistry ; DNA, Bacterial - chemistry ; DNA, Bacterial - metabolism ; DNA, Single-Stranded - chemistry ; DNA, Single-Stranded - metabolism ; Enzymes ; Enzymes and enzyme inhibitors ; Escherichia coli ; Escherichia coli Proteins - chemistry ; Escherichia coli Proteins - metabolism ; Eukaryotic Initiation Factor-4A ; Fluorescence ; Fluorescence Polarization ; Fourier Analysis ; Fundamental and applied biological sciences. Psychology ; Geometric Concepts ; Geometry ; Hydrogen Bonding ; INTERACTIONS ; Ligands ; Membrane Transport Proteins - chemistry ; Membrane Transport Proteins - metabolism ; Miscellaneous ; Models, Molecular ; Molecular biophysics ; Molecular Sequence Data ; NATIONAL SYNCHROTRON LIGHT SOURCE ; Nucleotide sequence ; NUCLEOTIDES ; Peptide Initiation Factors - chemistry ; Peptides - chemistry ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Precursors - metabolism ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein subunits ; Proteins ; SEC Translocation Channels ; Structure in molecular biology ; Temperature ; Topology</subject><ispartof>Science (American Association for the Advancement of Science), 2002-09, Vol.297 (5589), p.2018-2026</ispartof><rights>Copyright 2002 American Association for the Advancement of Science</rights><rights>2002 INIST-CNRS</rights><rights>COPYRIGHT 2002 American Association for the Advancement of Science</rights><rights>COPYRIGHT 2002 American Association for the Advancement of Science</rights><rights>Copyright American Association for the Advancement of Science Sep 20, 2002</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c803t-5af6dafe9ce4f883bad859cd0d50645a63862541a98cc7500404e5a8e658c7d83</citedby><cites>FETCH-LOGICAL-c803t-5af6dafe9ce4f883bad859cd0d50645a63862541a98cc7500404e5a8e658c7d83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3832427$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3832427$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>315,782,786,805,887,2888,2889,27933,27934,58026,58259</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=13957281$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12242434$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/15009157$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Hunt, John F.</creatorcontrib><creatorcontrib>Weinkauf, Sevil</creatorcontrib><creatorcontrib>Henry, Lisa</creatorcontrib><creatorcontrib>Fak, John J.</creatorcontrib><creatorcontrib>McNicholas, Paul</creatorcontrib><creatorcontrib>Oliver, Donald B.</creatorcontrib><creatorcontrib>Deisenhofer, Johann</creatorcontrib><creatorcontrib>Brookhaven National Laboratory, National Synchrotron Light Source (US)</creatorcontrib><title>Nucleotide Control of Interdomain Interactions in the Conformational Reaction Cycle of SecA</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>The SecA adenosine triphosphatase (ATPase) mediates extrusion of the amino termini of secreted proteins from the eubacterial cytosol based on cycles of reversible binding to the SecYEG translocon. We have determined the crystal structure of SecA with and without magnesium-adenosine diphosphate bound to the high-affinity ATPase site at 3.0 and 2.7 angstrom resolution, respectively. Candidate sites for preprotein binding are located on a surface containing the SecA epitopes exposed to the periplasm upon binding to SecYEG and are thus positioned to deliver preprotein to SecYEG. 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biochemistry</topic><topic>Anisotropy</topic><topic>ATPases</topic><topic>Bacillus subtilis - enzymology</topic><topic>Bacteria</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - metabolism</topic><topic>Base sequence</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>Binding Sites</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>BIOLOGICAL FUNCTIONS</topic><topic>Crystal structure</topic><topic>Crystalline structure</topic><topic>Crystallization</topic><topic>Crystallography</topic><topic>Crystallography, X-Ray</topic><topic>Dimerization</topic><topic>Dimers</topic><topic>DNA Helicases - chemistry</topic><topic>DNA, Bacterial - chemistry</topic><topic>DNA, Bacterial - metabolism</topic><topic>DNA, Single-Stranded - chemistry</topic><topic>DNA, Single-Stranded - metabolism</topic><topic>Enzymes</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Escherichia coli</topic><topic>Escherichia coli Proteins - 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Database</collection><collection>Research Library (Corporate)</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>Materials Science Collection</collection><collection>ProQuest One Education</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Engineering Collection</collection><collection>Environmental Science Collection</collection><collection>ProQuest Central Basic</collection><collection>University of Michigan</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Science (American Association for the Advancement of Science)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hunt, John F.</au><au>Weinkauf, Sevil</au><au>Henry, Lisa</au><au>Fak, John J.</au><au>McNicholas, Paul</au><au>Oliver, Donald B.</au><au>Deisenhofer, Johann</au><aucorp>Brookhaven National Laboratory, National Synchrotron Light Source (US)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nucleotide Control of Interdomain Interactions in the Conformational Reaction Cycle of SecA</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>2002-09-20</date><risdate>2002</risdate><volume>297</volume><issue>5589</issue><spage>2018</spage><epage>2026</epage><pages>2018-2026</pages><issn>0036-8075</issn><issn>0193-4511</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>The SecA adenosine triphosphatase (ATPase) mediates extrusion of the amino termini of secreted proteins from the eubacterial cytosol based on cycles of reversible binding to the SecYEG translocon. We have determined the crystal structure of SecA with and without magnesium-adenosine diphosphate bound to the high-affinity ATPase site at 3.0 and 2.7 angstrom resolution, respectively. Candidate sites for preprotein binding are located on a surface containing the SecA epitopes exposed to the periplasm upon binding to SecYEG and are thus positioned to deliver preprotein to SecYEG. Comparisons with structurally related ATPases, including superfamily I and II ATP-dependent helicases, suggest that the interaction geometry of the tandem motor domains in SecA is modulated by nucleotide binding, which is shown by fluorescence anisotropy experiments to reverse an endothermic domain-dissociation reaction hypothesized to gate binding to SecYEG.</abstract><cop>Washington, DC</cop><pub>American Association for the Advancement of Science</pub><pmid>12242434</pmid><doi>10.1126/science.1074424</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 2002-09, Vol.297 (5589), p.2018-2026 |
| issn | 0036-8075 0193-4511 1095-9203 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_743313993 |
| source | JSTOR Archive Collection A-Z Listing; MEDLINE; Science Magazine |
| subjects | Adenosine Diphosphate - chemistry Adenosine Diphosphate - metabolism Adenosine triphosphatase Adenosine triphosphatases Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - metabolism Adenosine Triphosphate - chemistry Adenosine Triphosphate - metabolism Amino Acid Motifs Amino Acid Sequence Analytical, structural and metabolic biochemistry Anisotropy ATPases Bacillus subtilis - enzymology Bacteria Bacterial Proteins - chemistry Bacterial Proteins - metabolism Base sequence BASIC BIOLOGICAL SCIENCES Binding Sites Biochemistry Biological and medical sciences BIOLOGICAL FUNCTIONS Crystal structure Crystalline structure Crystallization Crystallography Crystallography, X-Ray Dimerization Dimers DNA Helicases - chemistry DNA, Bacterial - chemistry DNA, Bacterial - metabolism DNA, Single-Stranded - chemistry DNA, Single-Stranded - metabolism Enzymes Enzymes and enzyme inhibitors Escherichia coli Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism Eukaryotic Initiation Factor-4A Fluorescence Fluorescence Polarization Fourier Analysis Fundamental and applied biological sciences. Psychology Geometric Concepts Geometry Hydrogen Bonding INTERACTIONS Ligands Membrane Transport Proteins - chemistry Membrane Transport Proteins - metabolism Miscellaneous Models, Molecular Molecular biophysics Molecular Sequence Data NATIONAL SYNCHROTRON LIGHT SOURCE Nucleotide sequence NUCLEOTIDES Peptide Initiation Factors - chemistry Peptides - chemistry Protein Binding Protein Conformation Protein Folding Protein Precursors - metabolism Protein Structure, Secondary Protein Structure, Tertiary Protein subunits Proteins SEC Translocation Channels Structure in molecular biology Temperature Topology |
| title | Nucleotide Control of Interdomain Interactions in the Conformational Reaction Cycle of SecA |
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