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__NOTOC__
<StructureSection load='1pjr' size='350' side='right' scene='' caption='DNA-dependent helicase PcrA (PDB code [[1pjr]])'>
<StructureSection load='1pjr' size='450' side='right' scene='' caption=''>
== Function ==
__NOTOC__
'''Helicase''' (Hel) is a motor protein which separates nucleic acid strands like DNA double helix or self-annealed RNA.  They use ATP hydrolysis for energy.  Hel falls into 5 superfamilies (SF1-SF5).  Some Hel contain a Helicase and RNase D C terminal
'''Helicase''' (Hel) is a motor protein which separates nucleic acid strands like DNA double helix or self-annealed RNA.  They use ATP hydrolysis for energy.  Hel falls into 5 superfamilies (SF1-SF5).  Some Hel contain a Helicase and RNase D C terminal
Domain (HRDC).  The α-thalassemia and mental retardation X-linked syndrome helicase (ATRX ), contains an ATRX-Dnmt3-Dnmt3L (ADD) domain in which many disease-related mutations are found.
Domain (HRDC).  The α-thalassemia and mental retardation X-linked syndrome helicase (ATRX ), contains an ATRX-Dnmt3-Dnmt3L (ADD) domain in which many disease-related mutations are found.<br />
 
*'''ATP-dependent helicase Rho''' is a protein involved in termination of transcription in prokaryotes.  Rho binds to the transcription terminator site on single-stranded RNA.  Rho forms a ring-shaped hexamer and advances along the mRNA until it reaches the RNA polymerase and causing it to dissociate from the DNA and end transcription.<br />
*'''ATP-dependent helicase RuvB-like 1''' (RuvBL1) or '''TIP49''' is a human protein which forms hexamers.  The hexamer forms dodecamer upon association with RuvBL2 or '''TIP48''' and the complex possesses single-stranded DNA-stimulated ATPase and helicase activities.
*'''ATP-dependent DNA helicase RecG''' or '''RecG''' is an ''E. coli'' protein which acts in recombination and repair of damaged DNA<ref>PMID:8428576</ref> .  RecG processes Holliday junctions to mature products.  See details in [[RecG Bound to Three-Way DNA Junction]].
*'''DnaB''' and '''DinG''' exhibit helicase and ATPase activities<ref>PMID:24387047</ref>.
*'''BLM helicase''' or '''Bloom syndrome protein''' can unwind DNA secondary structures<ref>PMID:37503837</ref>.
*'''Sen1 helicese''' has a role in transcription termination of nonpolyadenylated and polyadenylated RNA polymerase II transcripts<ref>PMID:21211720</ref>.
*'''Snf2 helicase''' and '''Swr1 helicase''' regulate the structure and dynamic properties of chromatin<ref>PMID:16738128</ref>.
*'''Ski2 helicase''' is involved in RNA processing and degradation<ref>PMID:22995828</ref>.
*'''XPD helicase''' or '''Rad3''' in yeast is a component of transcription factor IIH<ref>PMID:18510925</ref>.
*'''Cas3 helicase''' exhibits helicase, nuclease and ATPase activities<ref>PMID:25981480</ref>.
*'''Aquarius helicase''' is an RNA helicase that binds pre-mRNA introns to defined position<ref>PMID:25599396</ref>.
For details of PcrA helicase see<br />
For details of PcrA helicase see<br />
*[[Molecular Playground/PcrA Helicase]]<br />
*[[Molecular Playground/PcrA Helicase]]<br />
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For ATP-dependent helicase RecG see <br />
For ATP-dependent helicase RecG see <br />
*[[RecG Bound to Three-Way DNA Junction]]. <br />
*[[RecG Bound to Three-Way DNA Junction]]. <br />
For ATP-dependent helicase HepA see <br />
*[[RapA, a Swi2/Snf2 protein]]. <br />
For DEAD box ATP-dependent RNA helicase see <br />
For DEAD box ATP-dependent RNA helicase see <br />
*[[C-terminal domain of the DEAD-box protein Dbp5]]<br />
*[[C-terminal domain of the DEAD-box protein Dbp5]]<br />
Line 19: Line 30:
*[[Dead-box RNA helicase DDX19, in complex with an ATP-analogue and RNA]]. <br />
*[[Dead-box RNA helicase DDX19, in complex with an ATP-analogue and RNA]]. <br />
*[[Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa]]<br />
*[[Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa]]<br />
For helicase XPD see<br />
*[[XPD Helicase (3CRV)]]<br />
For helicase II or UvrD see<br />
*[[DNA Repair]]<br />
For SARS-CoV-2 helicase nsp13 see<br />
*[[SARS-CoV-2 enzyme Hel]]<br />
See also<br />
See also<br />
*[[Transcription and RNA Processing]]
*[[Transcription and RNA Processing]]
*[[Brr2]]
*[[Brr2]] - pre-mRNA-splicing helicase.


== What is a Helicase? ==
== What is a Helicase? ==
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{{clear}}
{{clear}}
PcrA is part of the replication machinery of the [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]a gram (+) bacteria, This helicase is part of the superfamily I of Helicases.  Monomeric protein that is mainly <scene name='User:Luis_E_Ramirez-Tapia/Sandbox_1/Initial/1'>alpha helical</scene> has the <scene name='User:Luis_E_Ramirez-Tapia/Sandbox_2/1pjrconser/2'>highly conserved</scene> Rec domians.  This helicase was reported as a mutation in the gen PcrA from [http://en.wikipedia.org/wiki/staphylococcu "Stapphylococcus aerous"], this mutation was related to a deficiency in the replication of a reporter plasmid.[http://www.ncbi.nlm.nih.gov/pubmed/8232203?ordinalpos=81&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum]
PcrA is part of the replication machinery of the [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]a gram (+) bacteria, This helicase is part of the superfamily I of Helicases.  Monomeric protein that is mainly <scene name='User:Luis_E_Ramirez-Tapia/Sandbox_1/Initial/1'>alpha helical</scene> has the <scene name='User:Luis_E_Ramirez-Tapia/Sandbox_2/1pjrconser/2'>highly conserved</scene> Rec domians.  This helicase was reported as a mutation in the gen PcrA from [http://en.wikipedia.org/wiki/staphylococcu "Stapphylococcus aerous"], this mutation was related to a deficiency in the replication of a reporter plasmid.[http://www.ncbi.nlm.nih.gov/pubmed/8232203?ordinalpos=81&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum]


<table align='right'><tr><td>&nbsp;</td><td>{{Template:ColorKey_ConSurf}}</td></tr></table>
<table align='right'><tr><td>&nbsp;</td><td>{{Template:ColorKey_ConSurf}}</td></tr></table>
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==PcrA Helicase Mechanism : The Mexican Wave==
==PcrA Helicase Mechanism : The Mexican Wave==
Professor Dale B. Wigley' group in 1996-1999 was able to crystalize the intermediate states from PcrA, giving solution to the controversy of what kind of mechanism this helicase has. [http://www.ncbi.nlm.nih.gov/pubmed/10199404ordinalpos=39&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum]
Professor Dale B. Wigley' group in 1996-1999 was able to crystalize the intermediate states from PcrA, giving solution to the controversy of what kind of mechanism this helicase has. [http://www.ncbi.nlm.nih.gov/pubmed/10199404ordinalpos=39&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum]
Two crystal form of the enzyma, one couple with a 10 mer DNA and a non hydrolizable form of ATP (ATPnP) (pdb id: [[3pjr]], <scene name='User:Luis_E_Ramirez-Tapia/Sandbox_2/3pjrinitial/1'> (Enzyme Subtrate Structure) </scene>and another a truncated form embebed in sulfate (pdb id: [[2pjr]]<scene name='User:Luis_E_Ramirez-Tapia/Sandbox_2/2pjrinitial/1'> (Enzyme Product Structure)</scene>, give a light in a model for how ATP hydrolysis results in motor movement along ssDNA. In the figure below step 1 (top) is the ATP free (product) ssDNA conformation. The DNA bases are labelled arbitrarily. On binding ATP, F626 creates a new binding pocket for base 6. Likewise, F64 destroys an acceptor pocket for base 2, forcing it to move to the position occupied by base 1. After ATP hydrolysis, the grip on base 6 is released. When the Y257 pocket is re-opened due to movement of F64, bases 3-6 can now flip through the acceptor pockets to their new positions. This model predicts that each ATP hydrolysis event will advance PcrA one base along ssDNA.[http://www.icnet.uk/labs/wigley/projects/helicase/35.html]
Two crystal form of the enzyma, one couple with a 10 mer DNA and a non hydrolizable form of ATP (ATPnP) (pdb id: [[3pjr]], <scene name='User:Luis_E_Ramirez-Tapia/Sandbox_2/3pjrinitial/1'> (Enzyme Substrate Structure) </scene>and another a truncated form embebed in sulfate (pdb id: [[2pjr]]<scene name='User:Luis_E_Ramirez-Tapia/Sandbox_2/2pjrinitial/1'> (Enzyme Product Structure)</scene>, give a light in a model for how ATP hydrolysis results in motor movement along ssDNA. In the figure below step 1 (top) is the ATP free (product) ssDNA conformation. The DNA bases are labelled arbitrarily. On binding ATP, F626 creates a new binding pocket for base 6. Likewise, F64 destroys an acceptor pocket for base 2, forcing it to move to the position occupied by base 1. After ATP hydrolysis, the grip on base 6 is released. When the Y257 pocket is re-opened due to movement of F64, bases 3-6 can now flip through the acceptor pockets to their new positions. This model predicts that each ATP hydrolysis event will advance PcrA one base along ssDNA.[http://www.icnet.uk/labs/wigley/projects/helicase/35.html]
[[Image:Mexicanwave.jpg|thumb|170px|left|Inchworm or Mexicanwave model]]
[[Image:Mexicanwave.jpg|thumb|170px|left|Inchworm or Mexicanwave model]]
[[Image:Snapshot_2008-12-03_14-11-31.jpg|thumb|400px|center|PcrA Movie]]
[[Image:Snapshot_2008-12-03_14-11-31.jpg|thumb|400px|center|PcrA Movie]]


'''The link below show a movie with the principal characteristics of this protain as long with the inchworm mode'''. [http://www.youtube.com/watch?v=fDwaWCkhgZI Pcr4 Helicase and Mexican Wave]
'''The link below show a movie with the principal characteristics of this protain as long with the inchworm mode'''. [http://www.youtube.com/watch?v=fDwaWCkhgZI Pcr4 Helicase and Mexican Wave]
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PcrA share structural domains with the Rec helicases, like UvrD ([[2is1]]) and RepD ([[1uaa]]) from E. coli, Superfamily 1 (SF1) helicases are probably the best characterized class, certainly from a structural perspective. All members characterized to date are bona fide helicases and α enzymes. Indeed, from their mode of translocation via the bases it is difficult to envisage how they could translocate along a duplex. However, they can have either A or B directional polarity.
PcrA share structural domains with the Rec helicases, like UvrD ([[2is1]]) and RepD ([[1uaa]]) from E. coli, Superfamily 1 (SF1) helicases are probably the best characterized class, certainly from a structural perspective. All members characterized to date are bona fide helicases and α enzymes. Indeed, from their mode of translocation via the bases it is difficult to envisage how they could translocate along a duplex. However, they can have either A or B directional polarity.
{{clear}}
{{clear}}
==3D structures of helicase==
[[Helicase 3D structures]]


</StructureSection>
</StructureSection>
==3D structures of helicase== 
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
[[3oc3]] – Hel MOT1 heat domain + TFIID-1 – ''Encephalitozoon cuniculi''<BR />
[[2p6r]] – AfHel 308 + DNA – ''Archaeoglobus fulgidus''<BR />
[[2p6u]] - AfHel 308
===DNA helicase===
[[3lfu]] – EcHel II – ''Escherichia coli''<BR />
[[2is1]], [[2is2]] - EcHel II (mutant) + DNA<BR />
[[2is4]], [[2is6]] - EcHel II (mutant) + ADP + DNA<BR />
[[3fld]] – EcHel I C terminal<BR />
[[2q7t]], [[2q7u]] – EcHel I relaxase domain (mutant) <BR />
[[1p4d]] - EcHel I relaxase domain<BR />
[[2a0i]] - EcHel I (mutant) + DNA<BR />
[[1q2z]], [[1rw2]] – hHel II KU86 C terminal – NMR<BR />
[[1e0j]], [[1e0k]] – Hel 4D domain – Phage T7
===ATP-dependent helicase ATRX===
[[3qln]] - hATRX ADD domain – human<BR />
[[2ld1]], [[2jm1]] - hATRX ADD domain - NMR<BR />
[[3ql9]] – hATRX ADD domain + histone H3 peptide <BR />
[[2lbm]] - hATRX ADD domain + histone H3 peptide – NMR<BR />
[[3qla]], [[3qlc]] - hATRX ADD domain (mutant) + histone H3 peptide<BR />
[[2xzp]] - hRENT1 helicase domain<BR />
[[2wjv]] - hRENT1 helicase CH and C terminal domains<BR />
[[2wjy]] - hRENT1 helicase CH domains<BR />
[[2xzo]] – hRENT1 helicase domain + RNA<BR />
===ATP-dependent helicase Rho===
[[3l0o]] – TmRho – ''Thermotoga maritima''<BR />
[[3ice]] – EcRho + ADP + BeF3 + RNA<BR />
[[2ht1]] - EcRho + RNA<BR />
[[1a8v]] – EcRho RNA-binding domain<br />
[[2a8v]] – EcRho RNA-binding domain + RNA<br />
[[1pv4]] – EcRho + DNA<br />
[[1pvo]] – EcRho + ssRNA + ANPPNP<br />
[[1xpr]], [[1xpu]] - EcRho + ssRNA + antibiotic
===ATP-dependent helicase MFD===
[[3hjh]] – EcMFD motor domain
===ATP-dependent helicase E1===
[[2v9p]] – PvE1 helicase domain – Bovine papillomavirus<br />
[[2gxa]] – PvE1 + DNA + Mg-ADP<br />
[[1tue]] – PvE1 + E2 – human papillomavirus
===ATP-dependent helicase CHD1===
[[2h1e]], [[2xb0]], [[3mwy]] – yCHD1 chromodomain<BR />
[[2dy7]] - yCHD1 chromodomain 1 – NMR<BR />
[[2dy8]] - yCHD1 chromodomain 2 – NMR<BR />
[[3ted]] - yCHD1 chromodomain 1 + DNA
===Dead box ATP-dependent RNA helicase===
[[3fho]] – DBP5 – fission yeast<BR />
[[2kbe]] – yDBP5 N terminal – NMR<BR />
[[2kbf]] - yDBP5 C terminal – NMR<BR />
[[3gfp]] - yDBP5 C-terminal<BR />
[[2i4i]] – hDDX3X<BR />
[[2jgn]] – hDDX3X helicase domain<BR />
[[3ly5]] – hDDX18 dead domain<BR />
[[2rb4]] – hDDX25 helicase domain<BR />
[[2p6n]] – hDDX41 helicase domain (mutant) <BR />
[[2e29]] - hDDX50 GUCT domain - NMR<BR />
[[2rqa]] – hDHX58 C terminal – NMR<BR />
[[3eqt]] - hDHX58 C terminal + RNA<BR />
[[2eqs]] – hDHX8 S1 domain<BR />
[[3i4u]]– hDHX8 residues 950-1183<br />
[[1vec]] – hP54 N terminal<BR />
[[2hjv]] – BsDBPA domain 2 – ''Bacillus subtilis''<BR />
[[2g0c]] - BsDBPA RNA-binding domain<br />
[[3eaq]], [[3ear]], [[3eas]] – TtHera residues 215-426 - ''Thermus thermophiles''<br />
[[3i31]] - TtHera residues 431-517<br />
[[3i32]] - TtHera residues 218-517<br />
[[3nej]] - TtHera N terminal (mutant)
===Dead box ATP-dependent RNA helicase complexes===
[[3rrm]] – yDBP5 residues 91-482 (mutant) + GLE1 + NUP159 + ADP + IP6 – yeast<BR />
[[3rrn]] - yDBP5 residues 91-482 (mutant) + GLE1 + IP6<BR />
[[3pew]], [[3pey]] - yDBP5 residues 91-482 (mutant) + ADP + BeF3 + RNA<BR />
[[3peu]], [[3pev]] - yDBP5 C-terminal (mutant) + GLE1 + IP6<BR />
[[3jrv]] – DDX3X + protein K7 – Vaccinia virus<BR />
[[3fmo]], [[3fhc]] – hDBP5 + Nup214<BR />
[[3fht]] – hDBP5 + AMPPNP + RNA<BR />
[[3fmp]] – hDDX19B + Nup214<br />
[[3g0h]] – hDDX19B residues 54-275 + ATP analog + RNA<BR />
[[3ews]] - hDDX19B residues 54-275 + ADP<BR />
[[3dkp]] – hDDX52 domain I + ADP<BR />
[[3tmi]] - hDHX58 residues 232-925 + RNA<br />
[[2wax]], [[2way]] – hDDX6 C terminal + EDC3-FDF peptide<BR />
[[2j0s]], [[2j0q]], [[2hyi]] – hDDX48 + protein mago nashi homolog + RNA-binding protein 8A + protein CASC3 + RNA<BR />
[[2j0u]] - hDDX48 + protein CASC3<BR />
[[2db3]] – VASA residues 200-623 + RNA – ''Drosophila melanogaster''<br />
[[3nbf]] - TtHera N terminal (mutant) + 8-oxo-ADP<br />
[[3moj]] - BsDBPA RNA-binding domain + RNA
===ATP-dependent RNA helicase===
[[2xzl]] – yNAM7 CH and helicase domains + RNA<BR />
[[2xgj]] – yDOB1 residues 81-1073 + RNA<BR />
[[3l9o]] - yDOB1 residues 1-1073 + peptide<BR />
[[2xau]], [[3kx2]] – yPRP43 + ADP<BR />
[[3i5x]], [[3i5y]] – yMSS116 residues 37-597 + AMPPNP + RNA<BR />
[[3sqw]], [[3sqx]] - yMSS116 residues 88-664 + AMPPNP + RNA<br />
[[3i61]] - yMSS116 residues 37-597 + ADP + BeF3 + RNA<BR />
[[3i62]] - yMSS116 residues 37-597 + ADP + AlF4 + RNA<BR />
[[2vso]], [[2vsx]] – yEIF4A + initiation factor 4F middle domain<BR />
[[2g9n]] - hEIF4A dead domain
===Viral ATP-dependent RNA helicase NS3===
[[3o8b]], [[3o8d]], [[1cu1]], [[8ohm]], [[1hei]] – HvHel NS3 – Hepatitis C virus<BR />
[[1onb]], [[1jr6]] - HvHel NS3 arginine-rich domain – NMR<BR />
[[2jlq]], [[2bhr]], [[2bmf]] – DvHel NS3 residues 1646-2092 – Dengue virus<BR />
[[2z83]] – Hel NS3 residues 167-624 – Japanese encephalitis virus<BR />
[[2v8o]], [[2wv9]] - Hel NS3 helicase domain – Murray valley encephalitis virus<BR />
[[2qeq]] - Hel NS3 residues 1691-2124 – Kunjin virus<BR />
[[2v6i]] – KvHel helicase domain – Kokobera virus<BR />
[[2v6j]] - KvHel helicase domain (mutant)
===Viral ATP-dependent RNA helicase NS3 complexes===
[[3o8c]], [[3o8r]], [[3kqh]], [[3kqk]], [[3kql]], [[3kqn]], [[3kqu]], [[1a1v]] - HvHel NS3 + RNA<BR />
[[2f9v]] - HvHel NS3 protease domain + polyprotein<BR />
[[2a4g]], [[1rtl]], [[1w3c]], [[1dxp]] - HvHel NS3 protease domain + NS4A peptide<BR />
[[2a4q]], [[2a4r]], [[2f9u]], [[2fm2]], [[1dy8]], [[1dy9]] - HvHel NS3 protease domain + NS4A peptide + inhibitor<BR />
[[2jlr]] - DvHel NS3 residues 1646-2092 + AMPPNP<BR />
[[2jls]] - DvHel NS3 residues 1646-2092 + ADP<BR />
[[2jlu]], [[2jlw]] - DvHel NS3 residues 1646-2092 + RNA<BR />
[[2jlv]] - DvHel NS3 residues 1646-2092 + AMPPNP + RNA<BR />
[[2jlx]], [[2jly]], [[2jlz]] - DvHel NS3 residues 1646-2092 + ADP + RNA<BR />
[[2vbc]] - DvHel NS3 residues 1475-2092 + NS2A peptide
===ATP-dependent RNA helicase SUV3===
[[3rc3]] – hSUV3 residues 47-722<BR />
[[3og8]] – hDDX58 C terminal + RNA<BR />
[[3rc8]] - hSUV3 residues 47-722 + RNA<BR />
===ATP-dependent RNA helicase A===
[[3llm]] – hHel A<BR />
[[1whq]] – Hel A RNA-binding domain – mouse - NMR<BR />
===ATP-dependent RNA helicase Repa===
[[1uaa]] – EcRepa + DNA<br />
[[1nlf]] - EcRepa + sulfate<br />
[[1g8y]], [[1olo]] - EcRepa
===ATP-dependent RNA helicase HEF===
[[1x2i]] – HEF DNA-binding domain – ''Pyrococcus furiosus''
===Werner syndrome ATP-dependent DNA helicase===
[[2e1e]], [[2e1f]], [[2dgz]] – hWRN HRDC domain<BR />
[[2fbt]] - hWRN exonuclease domain<BR />
[[2fbv]], [[2fbx]], [[2fby]], [[2fc0]] - hWRN exonuclease domain + metal ion
[[3aaf]] – hWRN C terminal + DNA<br />
[[2e6l]], [[2e6m]]- WRN exonuclease domain - mouse
===ATP-dependent DNA helicase Q===
[[2v1x]] - hQ1 residues 49-616<BR />
[[2wwy]] – hQ1 residues 49-616 + DNA<br />
[[2kmu]] – hQ4 N terminal - NMR
===ATP-dependent DNA helicase RecG===
[[1gm5]] – TmRecG  + DNA <BR />
===ATP-dependent DNA helicase RecQ===
[[3iuo]] – RecQ residues 604-725 – ''Porphyromonas gingivalis''<BR />
[[2rhf]]– RecQ HRDC domain 3 – ''Deinococcus radiodurans''<BR />
[[1wud]] - EcRecQ HRDC domain<BR />
[[1oyw]] - EcRecQ catalytic domain<BR />
[[1oyy]] - EcRecQ catalytic domain + ATP<BR />
[[1d8b]] - yRecQ HRDC domain - NMR<BR />
===ATP-dependent DNA helicase RuvA, RuvB===
[[2ztc]], [[2ztd]], [[2zte]], [[2h5x]] – MtRuvA – ''Mycobacterium tuberculosis''<BR />
[[1bvs]] - RuvA – ''Mycobacterium leprae''<BR />
[[1d8l]] – EcRuvA N terminal<BR />
[[1c7y]], [[1bdx]] – EcRuvA + DNA<BR />
[[1ixr]], [[1ixs]] – TtRuvA + RuvB (mutant) <BR />
[[1in4]] – TmRuvB<BR />
[[1in5]], [[1in6]], [[1in7]], [[1in8]], [[1j7k]] – TmRuvB (mutant)<br />
[[3pfi]] – RuvB + ADP – ''Campylobacter jejuni''
===ATP-dependent DNA helicase UVSW===
[[2oca]], [[1rif]]- T4UVSW (mutant) – Enterobacteria phage T4<BR />
[[2jpn]] - T4UVSW
===ATP-dependent DNA helicase UVRD===
[[2is1]] - EcUVRD + DNA
===ATP-dependent DNA helicase PriA===
[[2d7e]] – EcPriA DNA-binding domain<BR />
[[2d7g]], [[2d7h]], [[2dwl]], [[2dwm]], [[2dwn]] – EcPriA N terminal + polynucleotide
===ATP-dependent DNA helicase PcrA===
[[1qhg]] – GsPcrA (mutant) + ADPNP – ''Geobacillus stearothermophilus''<BR />
[[1qhh]] - GsPcrA + ADPNP<br />
[[2pjr]], [[3pjr]] - GsPcrA + DNA<br />
[[1pjr]] - GsPcrA
===DnaB helicase===
[[3gxv]] – HpDnaB – ''Helicobacter pylori''<BR />
[[4a1f]] – HpDnaB C terminal<br />
[[2vyf]] – GkDnaC – ''Geobacillus kaustophilus''<BR />
[[2r6d]] – BsDnaB – ''Bacillus stearothermophilus''<BR />
[[2r6e]], [[2r6d]] - GsDnaB <BR />
[[2r5u]] – MtDnaB N terminal<BR />
[[3bgw]] – BpDnaB-like – Bacillus phage SPP1<BR />
[[3bh0]] - BpDnaB-like G40P ATPase domain<BR />
[[2q6t]] – DnaB – ''Thermus aquaticus''<BR />
[[1mi8]] – DnaB – ''Synechocystis''<BR />
[[1b79]] - EcDnaB N terminal<BR />
[[1jwe]] - EcDnaB N terminal - NMR<BR />
[[2vye]] – GkDnaC + DNA<BR />
[[2r6c]], [[2r6a]] – BsDnaB + DnaG helicase-binding domain
===Helicase NSP2===
[[2hwk]] – NSP2 – Venzuelan equine encephalitis virus
===Helicase SNF2===
[[1z5z]] – SsSNF2 C terminal – ''Sulfolobus solfataricus''<br />
[[1z63]] - SsSNF2 ATPase core + DNA<br />
[[1z6a]] - SsSNF2 ATPase core
===Helicase SKI2===
[[2va8]] – SsSKI2<br />
[[4a4k]] – ySKI2 insertion domain<br />
[[4a4z]] – ySKI2 + AMPPNP
[[3crv]], [[3crw]] – XPD – ''Sulfolobus acidocaldarius''<br />
[[3hib]], [[3im1]], [[3im2]] – yBrr2 2nd SEC63 domain


==References==
==References==
Line 325: Line 86:
Betterton MD, Julicher F, "Opening of nucleic-acid double strands by helicases: active versus passive opening.", Physical Review E. 2005 Jan; 71 (1): 011904.<br />
Betterton MD, Julicher F, "Opening of nucleic-acid double strands by helicases: active versus passive opening.", Physical Review E. 2005 Jan; 71 (1): 011904.<br />
<ref group="xtra">PMID:16630817</ref><ref group="xtra">PMID:14747711</ref><references group="xtra"/>
<ref group="xtra">PMID:16630817</ref><ref group="xtra">PMID:14747711</ref><references group="xtra"/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
Line 338: Line 100:
[[Category: Helicase]]
[[Category: Helicase]]
[[Category: Sos response]]
[[Category: Sos response]]
*Created with the participation of [[User:Luis E Ramirez-Tapia|Luis E Ramirez-Tapia]], [[User:Wayne Decatur|Wayne Decatur]].
 
=='''Content Donators'''==
Created with the participation of [[User:Luis E Ramirez-Tapia|Luis E Ramirez-Tapia]], [[User:Wayne Decatur|Wayne Decatur]].
Retrieved from "https://proteopedia.org/Helicase"