Crystal Structure of the Helicase Domain from the Replicative Helicase-Primase of Bacteriophage T7
Identifieur interne : 003953 ( Main/Exploration ); précédent : 003952; suivant : 003954Crystal Structure of the Helicase Domain from the Replicative Helicase-Primase of Bacteriophage T7
Auteurs : Michael R. Sawaya [États-Unis] ; Shenyuan Guo [États-Unis] ; Stanley Tabor [États-Unis] ; Charles C. Richardson [États-Unis] ; Tom Ellenberger [États-Unis]Source :
- Cell [ 0092-8674 ] ; 1999.
English descriptors
- Teeft :
- Arginine, Arginine finger, Atpase, Bacteriophage, Biol, Ccp4, Central hole, Chem, Coli, Complementary strand, Conformational, Conformational changes, Crystal structure, Crystal structures, Crystallographic unit cell, Datp, Diffraction data, Dnab, Dnab family, Domain, Dttp, Duplex, Egelman, Electrostatic surface, Filament, Helical, Helical filament, Helicase, Helicase activity, Helicase domain, Helicase motif, Helicase motifs, Helicases, Helix, Hexamer, Hexameric, High protein concentrations, Hingorani, Hydrolysis, Methods enzymol, Motif, Notarnicola, Nucleotide, Nucleotide binding, Nucleotide hydrolysis, Patel, Pcra, Polymerase, Primase, Primase domain, Reca, Replication, Replication fork, Residue, Sequence motifs, Side chain, Subramanya, Subunit, Subunit interface, Unwinding, Unwinding activity, Water molecule.
Abstract
Abstract: Helicases that unwind DNA at the replication fork are ring-shaped oligomeric enzymes that move along one strand of a DNA duplex and catalyze the displacement of the complementary strand in a reaction that is coupled to nucleotide hydrolysis. The helicase domain of the replicative helicase-primase protein from bacteriophage T7 crystallized as a helical filament that resembles the Escherichia coli RecA protein, an ATP-dependent DNA strand exchange factor. When viewed in projection along the helical axis of the crystals, six protomers of the T7 helicase domain resemble the hexameric rings seen in electron microscopic images of the intact T7 helicase-primase. Nucleotides bind at the interface between pairs of adjacent subunits where an arginine is near the γ-phosphate of the nucleotide in trans. The bound nucleotide stabilizes the folded conformation of a DNA-binding motif located near the center of the ring. These and other observations suggest how conformational changes are coupled to DNA unwinding activity.
Url:
DOI: 10.1016/S0092-8674(00)81648-7
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream Istex, to step Corpus: 002680
- to stream Istex, to step Curation: 002680
- to stream Istex, to step Checkpoint: 001206
- to stream Main, to step Merge: 003998
- to stream Main, to step Curation: 003953
Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Crystal Structure of the Helicase Domain from the Replicative Helicase-Primase of Bacteriophage T7</title><author><name sortKey="Sawaya, Michael R" sort="Sawaya, Michael R" uniqKey="Sawaya M" first="Michael R." last="Sawaya">Michael R. Sawaya</name></author><author><name sortKey="Guo, Shenyuan" sort="Guo, Shenyuan" uniqKey="Guo S" first="Shenyuan" last="Guo">Shenyuan Guo</name></author><author><name sortKey="Tabor, Stanley" sort="Tabor, Stanley" uniqKey="Tabor S" first="Stanley" last="Tabor">Stanley Tabor</name></author><author><name sortKey="Richardson, Charles C" sort="Richardson, Charles C" uniqKey="Richardson C" first="Charles C." last="Richardson">Charles C. Richardson</name></author><author><name sortKey="Ellenberger, Tom" sort="Ellenberger, Tom" uniqKey="Ellenberger T" first="Tom" last="Ellenberger">Tom Ellenberger</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:83481F1C4404A2BE043C24C78B4128484B689F91</idno><date when="1999" year="1999">1999</date><idno type="doi">10.1016/S0092-8674(00)81648-7</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-Q5X4WRN4-Q/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">002680</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">002680</idno><idno type="wicri:Area/Istex/Curation">002680</idno><idno type="wicri:Area/Istex/Checkpoint">001206</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">001206</idno><idno type="wicri:doubleKey">0092-8674:1999:Sawaya M:crystal:structure:of</idno><idno type="wicri:Area/Main/Merge">003998</idno><idno type="wicri:Area/Main/Curation">003953</idno><idno type="wicri:Area/Main/Exploration">003953</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Crystal Structure of the Helicase Domain from the Replicative Helicase-Primase of Bacteriophage T7</title><author><name sortKey="Sawaya, Michael R" sort="Sawaya, Michael R" uniqKey="Sawaya M" first="Michael R." last="Sawaya">Michael R. Sawaya</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115</wicri:regionArea><wicri:noRegion>Massachusetts 02115</wicri:noRegion></affiliation></author><author><name sortKey="Guo, Shenyuan" sort="Guo, Shenyuan" uniqKey="Guo S" first="Shenyuan" last="Guo">Shenyuan Guo</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115</wicri:regionArea><wicri:noRegion>Massachusetts 02115</wicri:noRegion></affiliation></author><author><name sortKey="Tabor, Stanley" sort="Tabor, Stanley" uniqKey="Tabor S" first="Stanley" last="Tabor">Stanley Tabor</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115</wicri:regionArea><wicri:noRegion>Massachusetts 02115</wicri:noRegion></affiliation></author><author><name sortKey="Richardson, Charles C" sort="Richardson, Charles C" uniqKey="Richardson C" first="Charles C." last="Richardson">Charles C. Richardson</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115</wicri:regionArea><wicri:noRegion>Massachusetts 02115</wicri:noRegion></affiliation></author><author><name sortKey="Ellenberger, Tom" sort="Ellenberger, Tom" uniqKey="Ellenberger T" first="Tom" last="Ellenberger">Tom Ellenberger</name><affiliation wicri:level="1"><country wicri:rule="url">États-Unis</country></affiliation><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115</wicri:regionArea><wicri:noRegion>Massachusetts 02115</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Cell</title><title level="j" type="abbrev">CELL</title><idno type="ISSN">0092-8674</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1999">1999</date><biblScope unit="volume">99</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="167">167</biblScope><biblScope unit="page" to="177">177</biblScope></imprint><idno type="ISSN">0092-8674</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0092-8674</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Arginine</term><term>Arginine finger</term><term>Atpase</term><term>Bacteriophage</term><term>Biol</term><term>Ccp4</term><term>Central hole</term><term>Chem</term><term>Coli</term><term>Complementary strand</term><term>Conformational</term><term>Conformational changes</term><term>Crystal structure</term><term>Crystal structures</term><term>Crystallographic unit cell</term><term>Datp</term><term>Diffraction data</term><term>Dnab</term><term>Dnab family</term><term>Domain</term><term>Dttp</term><term>Duplex</term><term>Egelman</term><term>Electrostatic surface</term><term>Filament</term><term>Helical</term><term>Helical filament</term><term>Helicase</term><term>Helicase activity</term><term>Helicase domain</term><term>Helicase motif</term><term>Helicase motifs</term><term>Helicases</term><term>Helix</term><term>Hexamer</term><term>Hexameric</term><term>High protein concentrations</term><term>Hingorani</term><term>Hydrolysis</term><term>Methods enzymol</term><term>Motif</term><term>Notarnicola</term><term>Nucleotide</term><term>Nucleotide binding</term><term>Nucleotide hydrolysis</term><term>Patel</term><term>Pcra</term><term>Polymerase</term><term>Primase</term><term>Primase domain</term><term>Reca</term><term>Replication</term><term>Replication fork</term><term>Residue</term><term>Sequence motifs</term><term>Side chain</term><term>Subramanya</term><term>Subunit</term><term>Subunit interface</term><term>Unwinding</term><term>Unwinding activity</term><term>Water molecule</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Helicases that unwind DNA at the replication fork are ring-shaped oligomeric enzymes that move along one strand of a DNA duplex and catalyze the displacement of the complementary strand in a reaction that is coupled to nucleotide hydrolysis. The helicase domain of the replicative helicase-primase protein from bacteriophage T7 crystallized as a helical filament that resembles the Escherichia coli RecA protein, an ATP-dependent DNA strand exchange factor. When viewed in projection along the helical axis of the crystals, six protomers of the T7 helicase domain resemble the hexameric rings seen in electron microscopic images of the intact T7 helicase-primase. Nucleotides bind at the interface between pairs of adjacent subunits where an arginine is near the γ-phosphate of the nucleotide in trans. The bound nucleotide stabilizes the folded conformation of a DNA-binding motif located near the center of the ring. These and other observations suggest how conformational changes are coupled to DNA unwinding activity.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><country name="États-Unis"><noRegion><name sortKey="Sawaya, Michael R" sort="Sawaya, Michael R" uniqKey="Sawaya M" first="Michael R." last="Sawaya">Michael R. Sawaya</name></noRegion><name sortKey="Ellenberger, Tom" sort="Ellenberger, Tom" uniqKey="Ellenberger T" first="Tom" last="Ellenberger">Tom Ellenberger</name><name sortKey="Ellenberger, Tom" sort="Ellenberger, Tom" uniqKey="Ellenberger T" first="Tom" last="Ellenberger">Tom Ellenberger</name><name sortKey="Guo, Shenyuan" sort="Guo, Shenyuan" uniqKey="Guo S" first="Shenyuan" last="Guo">Shenyuan Guo</name><name sortKey="Richardson, Charles C" sort="Richardson, Charles C" uniqKey="Richardson C" first="Charles C." last="Richardson">Charles C. Richardson</name><name sortKey="Tabor, Stanley" sort="Tabor, Stanley" uniqKey="Tabor S" first="Stanley" last="Tabor">Stanley Tabor</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 003953 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 003953 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= MersV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= ISTEX:83481F1C4404A2BE043C24C78B4128484B689F91
|texte= Crystal Structure of the Helicase Domain from the Replicative Helicase-Primase of Bacteriophage T7
}}
| This area was generated with Dilib version V0.6.33. |  |