Helicase

spinqualitylabelsall models DNA-dependent helicase PcrA (PDB code 1pjr) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function 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. 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. For details of PcrA helicase see Molecular Playground/PcrA Helicase PcrA helicase. For ATP-dependent helicase Rho see Transcription Termination Factor Rho. For ATP-dependent helicase Q see Human RecQ-Like protein 1. For ATP-dependent helicase RecG see RecG Bound to Three-Way DNA Junction. For ATP-dependent helicase HepA see RapA, a Swi2/Snf2 protein. For DEAD box ATP-dependent RNA helicase see C-terminal domain of the DEAD-box protein Dbp5 DEAD-box RNA-helicase DDX19 in complex with ADP Dead-box RNA helicase DDX19, in complex with an ATP-analogue and RNA. Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa For helicase XPD see XPD Helicase (3CRV) See also Transcription and RNA Processing Brr2 - pre-mRNA-splicing helicase. What is a Helicase? Spacefill Helicases are nucleic acid–dependent ATP-ases that are capable of unwinding DNA [1] or RNA [2] duplex substrates. As a consequence, they play roles in almost every process in cells that involves nucleic acids, including DNA replication and repair, transcription, translation, ribosome synthesis (1). PcrA a Simple Model for Helicases PcrA_Structure PcrA is part of the replication machinery of the Geobacillus stearothermophilusa gram (+) bacteria, This helicase is part of the superfamily I of Helicases. Monomeric protein that is mainly alpha helical has the highly conserved Rec domians. This helicase was reported as a mutation in the gen PcrA from "Stapphylococcus aerous", this mutation was related to a deficiency in the replication of a reporter plasmid.[3] PcrA Biochemistry PcrA is has an ATPas activityt which directionality is from 3' to 5' helicase strand separation reaction. The enzyme shows a specificity for the DNA substrate in gel mobility assays with the preferred substrate being one containing both single and double stranded regions of DNA. In contrast to Rep and UvrD from E. coli, there is not evidence for dimerisation of the enzyme using gel filtration, or by crosslinking in the presence of combinations of Mg2+, nucleotides and DNA. Moreover, kcat for ATP hydrolysis is constant over a large range of protein concentrations. Therefore, the protein appears to be monomeric under all conditions tested, including in the structure of two crystal forms of PcrA.[4] 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. [5] Two crystal form of the enzyma, one couple with a 10 mer DNA and a non hydrolizable form of ATP (ATPnP) (pdb id: 3pjr, (Enzyme Subtrate Structure) and another a truncated form embebed in sulfate (pdb id: 2pjr (Enzyme Product Structure), 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.[6] Inchworm or Mexicanwave model PcrA Movie The link below show a movie with the principal characteristics of this protain as long with the inchworm mode. Pcr4 Helicase and Mexican Wave The Superfamily 1 (SF1) 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.

3D structures of helicase

Updated on 20-June-2018

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• Helicase Mot1
  • Molecular Playground/PcrA Helicase – Hel MOT1 heat domain + TFIID-1 – Encephalitozoon cuniculi
    
• Helicase 308
  • PcrA helicase – AfHel 308 + DNA – Archaeoglobus fulgidus
    
  • Transcription Termination Factor Rho - AfHel 308
• DNA helicase
  • Human RecQ-Like protein 1 – EcHel I C terminal – Escherichia coli
    
  • RecG Bound to Three-Way DNA Junction – EcHel I translocation domain
    
  • RapA, a Swi2/Snf2 protein, C-terminal domain of the DEAD-box protein Dbp5 – EcHel I relaxase domain (mutant)
    
  • DEAD-box RNA-helicase DDX19 in complex with ADP - EcHel I relaxase domain
    
  • Dead-box RNA helicase DDX19, in complex with an ATP-analogue and RNA, Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa - EcHel I + DNA
    
  • XPD Helicase (3CRV) - EcHel I (mutant) + DNA
    
  • Transcription and RNA Processing, Brr2 – Hel 4D domain – Phage T7
• DNA helicase II or UvrD
  • 3pjr – EcHel II
    
  • 2pjr, 2is1 - EcHel II (mutant) + DNA
    
  • 1uaa, 2is6 - EcHel II (mutant) + ADP + DNA
    
  • 4c2t, 4c2u, 4c30 – DrHel II + DNA - Deinococcus radiodurans
    
  • 1q2z, 1rw2 – hHel II KU86 C terminal – NMR
    
  • 5y58 – yHel II + DNA – yeast
    
  • 5y59 – yHel II subunit 2 + Sir4P peptide
    
• ATP-dependent helicase ATRX
  • 3qln - hATRX ADD domain residues 167-289 – human
    
  • 2ld1, 2jm1 - hATRX ADD domain - NMR
    
  • 3ql9, 4w5a – hATRX ADD domain + histone H3 peptide
    
  • 2lbm - hATRX ADD domain + histone H3 peptide – NMR
    
  • 3qla, 3qlc - hATRX ADD domain (mutant) + histone H3 peptide
    
  • 2xzp - hRENT1 helicase domain
    
  • 2wjv - hRENT1 helicase CH and C terminal domains
    
  • 2wjy - hRENT1 helicase CH domains
    
  • 2xzo – hRENT1 helicase domain + RNA
    
• ATP-dependent helicase Fun30
  • 5gn1 – yFun C-terminal
    
• ATP-dependent helicase Rho
  • 3l0o – TmRho – Thermotoga maritima
    
  • 3ice – EcRho + ADP + BeF3 + RNA
    
  • 2ht1 - EcRho + RNA
    
  • 1a8v, 1a62 – EcRho RNA-binding domain
    
  • 1a63 - EcRho RNA-binding domain – NMR
    
  • 2a8v – EcRho RNA-binding domain + RNA
    
  • 1pv4 – EcRho + DNA
    
  • 1pvo – EcRho + ssRNA + ANPPNP
    
  • 1xpr, 1xpu, 1xpo - EcRho + ssRNA + antibiotic
• ATP-dependent helicase MFD
  • 3hjh – EcMFD motor domain
• ATP-dependent helicase HEPA
  • 6bog – EcHEPA
• ATP-dependent helicase E1
  • 2v9p – PvE1 helicase domain – Bovine papillomavirus
    
  • 2gxa – PvE1 + DNA + Mg-ADP
    
  • 1tue – PvE1 + E2 – human papillomavirus
• ATP-dependent helicase CHD
  • 2h1e, 2xb0, 3mwy – yCHD1 chromodomain
    
  • 2dy7 - yCHD1 chromodomain 1 – NMR
    
  • 2dy8 - yCHD1 chromodomain 2 – NMR
    
  • 3ted - yCHD1 chromodomain 1 + DNA
    
  • 2b2y – hCHD1
    
  • 4b4c – hCHD1 DNA-binding domain
    
  • 2b2t, 2b2u, 2b2v, 2b2w – hCHD1 (mutant) + histone H3 tail
    
  • 4nw2 – hCHD1 + NS1 peptide
    
  • 2ee1 – hCHD4 chromodomain – NMR
    
  • 2l5u – hCHD4 PHD1 domain – NMR
    
  • 2l75 – hCHD4 PHD2 domain + histone H3 peptide– NMR
    
  • 2epb – hCHD6 chromodomain – NMR
    
  • 2ckc, 2v0e, 2v0f – hCHD7 BRK domain - NMR
    
  • 2dl6 – hCHD8 BRK domain - NMR
    
  • 2cka – hCHD8
    
• ATP-dependent DNA helicase PIF1

• • 5fhh – hPIF residues 200-641
    
  • 5o6b, 5o6d – yPIF residues 237-780 + DNA + ATP
    
  • 5o6e – yPIF residues 237-780 + DNA + ADP
    
• ATP-dependent DNA helicase TA0057

• • 5h8w – TaTA0 + DNA – Thermoplasma acidophilum
    
• ATP-dependent DNA helicase LHR

• • 5v9x – LHR + DNA – Mycobacterium smegmatis
    
• Dead box ATP-dependent RNA helicase
  • 3fho – DBP5 – fission yeast
    
  • 2kbe – yDBP5 N terminal – NMR
    
  • 2kbf - yDBP5 C terminal – NMR
    
  • 3gfp - yDBP5 C-terminal
    
  • 4xw3 – hDDX1 SPRY domain
    
  • 2i4i – hDDX3X residues 167-581
    
  • 4px9 - hDDX3X residues 135-407
    
  • 4pxa - hDDX3X residues 135-407 (mutant)
    
  • 5e7i - hDDX3X residues 133-584
    
  • 2jgn – hDDX3X helicase domain residues 408-579
    
  • 3ly5 – hDDX18 dead domain
    
  • 2rb4 – hDDX25 helicase domain
    
  • 2p6n – hDDX41 helicase domain (mutant)
    
  • 2e29, 2m3d - hDDX50 GUCT domain - NMR
    
  • 1vec – hP54 N terminal
    
  • 2hjv – BsDBPA domain 2 – Bacillus subtilis
    
  • 2g0c - BsDBPA RNA-binding domain
    
  • 3eaq, 3ear, 3eas – TtHera residues 215-426 - Thermus thermophilus
    
  • 3i31 - TtHera residues 431-517
    
  • 3i32 - TtHera residues 218-517
    
  • 3nej - TtHera N terminal (mutant)
    
  • 5ivl – GsDB CSHA - Geobacillus stearothermophilus
    
  • 5b88 - EcDBP RRM-like domain - NMR
    
  • 5gju - EcDBP residues 6-210
    
  • 5gi4 - EcDBP residues 218-445
    
• Dead box ATP-dependent RNA helicase complexes
  • 3rrm – yDBP5 residues 91-482 (mutant) + GLE1 + NUP159 + ADP + IP6
    
  • 3rrn - yDBP5 residues 91-482 (mutant) + GLE1 + IP6
    
  • 5elx - yDBP5 residues 91-482 + RNA
    
  • 3pew, 3pey - yDBP5 residues 91-482 (mutant) + ADP + BeF3 + RNA
    
  • 3peu, 3pev - yDBP5 C-terminal (mutant) + GLE1 + IP6
    
  • 3i5x, 3i5y – yMSS116 + AMPPNP + RNA
    
  • 3sqw, 3sqx - yMSS116 + AMPPNP + RNA
    
  • 3i61, 4tyw, 4tyy, 4tz0, 4tz6 - yMSS116 + nucleotide + BeF3 + RNA
    
  • 3i62 - yMSS116 + ADP + AlF4 + RNA
    
  • 4tyn - yMSS116 + ADP + DNA
    
  • 2xau, 3kx2, 5jpt – yPrp43 + nucleotide
    
  • 5i8q - yPrp43 + ADPNP + RNA
    
  • 5ltk, 5ltj, 5d0u - CtPrp43 + ADP – Chaetomium thermophilum
    
  • 5lta - CtPrp43 + ADP + RNA
    
  • 3jrv – DDX3X + protein K7 – Vaccinia virus
    
  • 3fmo, 3fhc – hDBP5 + Nup214
    
  • 3fht – hDBP5 + AMPPNP + RNA
    
  • 3fmp – hDDX19B + Nup214
    
  • 3g0h – hDDX19B residues 54-275 + ATP analog + RNA
    
  • 3ews - hDDX19B residues 54-275 + ADP
    
  • 5e7m, 5e7j – hDDX3X catalytic domain + nucleotide
    
  • 3dkp – hDDX52 domain I + ADP
    
  • 2wax, 2way – hDDX6 C terminal + EDC3-FDF peptide
    
  • 2j0s, 2j0q, 2hyi – hDDX48 + protein mago nashi homolog + RNA-binding protein 8A + protein CASC3 + RNA
    
  • 2j0u - hDDX48 + protein CASC3
    
  • 2db3 – DmVASA residues 200-623 + RNA – Drosophila melanogaster
    
  • 5nt7 – DmVASA RecA-like domain + maternal effect protein
    
  • 3nbf - TtHera N terminal (mutant) + 8-oxo-ADP
    
  • 3moj - BsDBPA RNA-binding domain + RNA
• DEAH box RNA helicase
  • 2eqs – hDHX8 S1 domain
    
  • 3i4u – hDHX8 residues 950-1183
    
  • 3llm – hDHX9
    
  • 2rs6, 2rs7 – DHX9 RNA-binding domain – mouse – NMR
    
  • 5xdr – hDHX15 residues 110-795 (mutant)
    
  • 2n16 – hDHX36 G-quadruplex domain - NMR
    
  • 2rqa – hDHX58 C terminal – NMR
    
  • 3vyx, 3vyy – hDHX9 RNA-binding domain + RNA
    
  • 2n21 – hDHX36 G-quadruplex domain + DNA - NMR
    
  • 5e3h - hDHX58 residues 232-925 + RNA
    
  • 3eqt- hDHX58 residues 541-678 + RNA
    
  • 5vha – bDHX36 residues 150-1010 - bovine
    
  • 5vhc, 5vhd – bDHX36 residues 150-1010 + ADP
    
  • 5vhe – bDHX36 residues 56-1010 + DNA
    
• ATP-dependent RNA helicase
  • 2xzl – yNAM7 CH and helicase domains + RNA
    
  • 2xgj – yDOB1 residues 81-1073 + RNA
    
  • 4u4c - yDOB1 residues 81-1073 + poly(A) RNA polymerase protein 2
    
  • 4qu4 - yDOB1
    
  • 5oob - yDOB1 residues 81-1073 + NOP53
    
  • 5suq – ySUB2 + TEX1 + THO2
    
  • 5sup – ySUB2 + YRA1 + RNA
    
  • 2vso, 2vsx – yEIF4A + initiation factor 4F middle domain
    
  • 2g9n - hEIF4A dead domain
• Viral ATP-dependent RNA helicase NS3
  • 3o8b, 3o8d, 1cu1, 8ohm, 1hei, 4a92, 3rvb – HvHel NS3 residues 1186-1658 – Hepatitis C virus
    
  • 1onb, 1jr6 - HvHel NS3 arginine-rich domain residues 1353-1507 – NMR
    
  • 2jlq, 2bhr, 2bmf, 2whx, 2wzq – DvHel NS3 residues 1646-2092 – Dengue virus
    
  • 5xc7 – DvHel NS3 residues 1646-2092 (mutant)
    
  • 2z83 – Hel NS3 residues 167-624 – Japanese encephalitis virus
    
  • 2v8o, 2wv9 - Hel NS3 helicase domain – Murray valley encephalitis virus
    
  • 2qeq - Hel NS3 residues 1691-2124 – Kunjin virus
    
  • 5txg, 5jmt, 5vi7, 5jps - ZvHel NS3 helicase domain – Zika virus
    
  • 5k8u, 5k8l, 5k8i, 5jwh, 5jrz - ZvHel NS3 residues 164-621
    
  • 5x8y - ZvHel NS1 residues 168-352
    
  • 2v6i – KvHel helicase domain – Kokobera virus
    
  • 2v6j - KvHel helicase domain (mutant)
    
  • 5wso, 5gvu - Hel NS3 residues 1939-2414 – bovine viral diarrhea virus
    
• Viral ATP-dependent RNA helicase NS3 complexes
  • 3o8c, 3o8r, 3kqh, 3kqk, 3kql, 3kqn, 3kqu, 1a1v - HvHel NS3 + RNA
    
  • 2f9v - HvHel NS3 protease domain + polyprotein
    
  • 2a4g, 1rtl, 1w3c, 1dxp - HvHel NS3 protease domain + NS4A peptide
    
  • 2a4q, 2a4r, 2f9u, 2fm2, 1dy8, 1dy9 - HvHel NS3 protease domain + NS4A peptide + inhibitor
    
  • 2jlr - DvHel NS3 residues 1646-2092 + AMPPNP
    
  • 2jls - DvHel NS3 residues 1646-2092 + ADP
    
  • 2jlu, 2jlw, 5xc6 - DvHel NS3 residues 1646-2092 + RNA
    
  • 2jlv - DvHel NS3 residues 1646-2092 + AMPPNP + RNA
    
  • 2jlx, 2jly, 2jlz - DvHel NS3 residues 1646-2092 + ADP + RNA
    
  • 2vbc - DvHel NS3 residues 1475-2092 + NS2A peptide
    
  • 5k8t - ZvHel NS3 residues 164-621 + GTP
    
  • 5gjc - ZvHel NS3 residues 1676-2119 + ATP
    
  • 5gjb - ZvHel NS3 residues 1676-2119 + RNA
    
  • 5y4z - ZvHel NS3 residues 1676-2119 + AMPPNP
    
• ATP-dependent RNA helicase SUV3
  • 3rc3 – hSUV3 residues 47-722
    
  • 3og8 – hDDX58 C terminal + RNA
    
  • 3rc8 - hSUV3 residues 47-722 + RNA
    
  • 6f4a – ySUV3 + exoribonuclease II + RNA
    
• ATP-dependent RNA helicase A
  • 3llm – hHel A
    
  • 3vyx, 3vyy - hHel A RNA-binding domain + RNA
    
  • 1whq, 2rs6, 2rs7 – Hel A RNA-binding domain – mouse - NMR
    
• ATP-dependent RNA helicase Repa
  • 1uaa – EcRepa + DNA
    
  • 1nlf - EcRepa + sulfate
    
  • 1g8y, 1olo - EcRepa
• ATP-dependent RNA helicase HEF
  • 1x2i – HEF DNA-binding domain – Pyrococcus furiosus
• ATP-dependent RNA helicase Srmb
  • 2yjt - EcSrmb residues 219-388 + RRAA
    
• ATP-dependent RNA helicase Dhh1
  • 4bru – yDhh1 (mutant) + EDC3
    
  • 4brw – yDhh1 (mutant) + PAT1
    
• Werner syndrome ATP-dependent DNA helicase
  • 2e1e, 2e1f, 2dgz – hWRN HRDC domain
    
  • 2fbt - hWRN exonuclease domain
    
  • 2fbv, 2fbx, 2fby, 2fc0 - hWRN exonuclease domain + metal ion
  • 3aaf – hWRN C terminal + DNA
    
  • 2e6l, 2e6m- WRN exonuclease domain - mouse
• ATP-dependent DNA helicase Q
  • 2v1x - hQ1 residues 49-616
    
  • 2wwy, 4u7d – hQ1 residues 49-616 + DNA
    
  • 5lst – hQ4 residues 427-1116
    
  • 2kmu – hQ4 N terminal - NMR
    
  • 5lb8 – hQ5
    
  • 5lb5, 5lb3 – hQ5 + ADP
    
  • 5lba – hQ5 + urea derivative
    
• ATP-dependent DNA helicase RecG
  • 1gm5 – TmRecG + DNA
    
• ATP-dependent DNA helicase RecQ (Bloom Syndrome helicase)
  • 3iuo – RecQ residues 604-725 – Porphyromonas gingivalis
    
  • 2rhf – DrRecQ HRDC domain 3 – Deinococcus radiodurans
    
  • 2ma1 - DrRecQ HRDC domain – NMR
    
  • 4q48 - DrRecQ catalytic domain
    
  • 4q47 - DrRecQ catalytic domain + ADP
    
  • 1wud - EcRecQ HRDC domain
    
  • 1oyw - EcRecQ catalytic domain
    
  • 1oyy - EcRecQ catalytic domain + ATP
    
  • 1d8b - yRecQ HRDC domain - NMR
    
  • 4cgz, 4o3m - hRecQ catalytic domain + DNA
    
  • 4cdg - hRecQ catalytic domain + nanobody
    
• ATP-dependent DNA helicase RuvA, RuvB
  • 2ztc, 2ztd, 2zte, 2h5x – MtRuvA – Mycobacterium tuberculosis
    
  • 1bvs - RuvA – Mycobacterium leprae
    
  • 1cuk, 1hjp – EcRuvA
    
  • 1d8l – EcRuvA N terminal
    
  • 1c7y, 1bdx – EcRuvA + DNA
    
  • 1hqc – TtRuvB
    
  • 1ixr, 1ixs – TtRuvA + RuvB (mutant)
    
  • 1in4 – TmRuvB
    
  • 1in5, 1in6, 1in7, 1in8, 1j7k – TmRuvB (mutant)
    
  • 3pfi – RuvB + ADP – Campylobacter jejuni
    
  • 6blb - PaRuvB + ADP - Pseudomonas aeruginosa
    
• ATP-dependent DNA helicase UVSW
  • 2oca, 1rif- T4UVSW (mutant) – Enterobacteria phage T4
    
  • 2jpn - T4UVSW
• ATP-dependent DNA helicase DDA
  • 3upu – T4DDA + DNA
    
• ATP-dependent DNA helicase PriA
  • 2d7e – EcPriA DNA-binding domain
    
  • 2d7g, 2d7h, 2dwl, 2dwm, 2dwn – EcPriA N terminal + polynucleotide
• ATP-dependent DNA helicase PcrA
  • 1qhg – GsPcrA (mutant) + ADPNP
    
  • 1qhh - GsPcrA + ADPNP
    
  • 2pjr, 3pjr - GsPcrA + DNA
    
  • 1pjr - GsPcrA
    
  • 5dma – GsPcrA C-terminal tudor domain
    
• DnaB helicase
  • 3gxv – HpDnaB – Helicobacter pylori
    
  • 4a1f – HpDnaB C terminal
    
  • 2r6d – BsDnaB – Bacillus stearothermophilus
    
  • 2r6e, 2r6d - GsDnaB
    
  • 2r5u – MtDnaB N terminal
    
  • 3bgw – BpDnaB-like – Bacillus phage SPP1
    
  • 3bh0 - BpDnaB-like G40P ATPase domain
    
  • 2q6t – DnaB – Thermus aquaticus
    
  • 1mi8 – DnaB – Synechocystis
    
  • 1b79 - EcDnaB N terminal
    
  • 1jwe - EcDnaB N terminal - NMR
    
  • 2r6c, 2r6a – BsDnaB + DnaG helicase-binding domain
• DnaC helicase
  • 2vyf– GkDnaC – Geobacillus kaustophilus
    
  • 2vye – GkDnaC + DNA
    
  • 3ec2 – AaDnaC – Aquifex aeolicus
    
  • 3ecc – AaDnaC + ADP
    
• Helicase BLM
  • 5lut – BLM DHBN domain - chicken
    
  • 5lus – BLM DHBN domain - pelican
    
  • 5lup – hBLM DHBN domain
    
• Helicase CA8 or Prp28
  • 4w7s – yCa8
    
• Helicase NSP2
  • 2hwk – NSP2 – Venzuelan equine encephalitis virus
• Helicase SEN1
  • 5mzn – ySEN1
    
• Helicase SNF2
  • 1z5z – SsSNF2 C terminal – Sulfolobus solfataricus
    
  • 1z63 - SsSNF2 ATPase core + DNA
    
  • 1z6a - SsSNF2 ATPase core
• Helicase SKI2
  • 2va8 – SsSKI2
    
  • 4a4k – ySKI2 insertion domain
    
  • 4a4z – ySKI2 + AMPPNP
• Helicase SWR1
  • 5i9e – ySWR1 + actin + actin-related protein
    
• Helicase XPD
  • 3crv, 3crw, 5h8c – XPD – Sulfolobus acidocaldarius
    
  • 4a15 - TaXPD + DNA
    
  • 2vsf - TaXPD
    
  • 2vl7 - XPD - Sulfolobus tokodaii
    
  • 5ivw - hXPD + XPB + TFIIH ubunits 2,3,4,5 + SCP-X + SCP-Ybr />
• Pre-mRNA-splicing Helicase
  • 3hib, 3im1, 3im2 – yBrr2 2nd SEC63 domain
    
  • 4bgd, 5m5p, 5m52, 5dca – yBrr2 + pre-mRNA-splicing factor 8
    
• crispr-associated helicase Cas3
  • 4q2c – TteCas3 – Thermobaculum terrenum
    
  • 4q2d – TteCas3 + DTP
    
  • 4qqw, 4qqx – TfCas3 – Thermobifida fusca
    
  • 4qqy – TfCas3 + ADP + HD nuclease
    
  • 4qqz – TfCas3 + AMPPNP
    
  • 5gqh – PaCas3 + anti-crispr protein 3
    
  • 5b7i – PaCas3 + ACRF3
    

References

Crystal structure of a DExx box DNA helicase., Subramanya HS, Bird LE, Brannigan JA, Wigley DB, Nature. 1996 Nov 28;384(6607):379-83. PMID:8934527
^ Johnson DS, Bai L, Smith BY, Patel SS, Wang MD (2007). "Single-molecule studies reveal dynamics of DNA unwinding by the ring-shaped t7 helicase". Cell 129 (7): 1299–309. doi:10.1016/j.cell.2007.04.038. PMID 17604719.
^ a b "Researchers solve mystery of how DNA strands separate" (2007-07-03). Retrieved on 2007-07-05.
^ Dumont S, Cheng W, Serebrov V, Beran RK, Tinoco Jr I, Pylr AM, Bustamante C, "RNA Translocation and Unwinding Mechanism of HCV NS3 Helicase and its Coordination by ATP", Nature. 2006 Jan 5; 439: 105-108. Anand SP, Zheng H, Bianco PR, Leuba SH, Khan SA. DNA helicase activity of PcrA is not required for displacement of RecA protein from DNA or inhibition of RecA-mediated DNA strand exchange. Journal of Bacteriology (2007) 189 (12):4502-4509.
Bird L, Subramanya HS, Wigley DB, "Helicases: a unifying structural theme?", Current Opinion in Structural Biology. 1998 Feb; 8 (1): 14-18.
Betterton MD, Julicher F, "Opening of nucleic-acid double strands by helicases: active versus passive opening.", Physical Review E. 2005 Jan; 71 (1): 011904.

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