2qkb: Difference between revisions
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|PDB= 2qkb |SIZE=350|CAPTION= <scene name='initialview01'>2qkb</scene>, resolution 2.40Å | |PDB= 2qkb |SIZE=350|CAPTION= <scene name='initialview01'>2qkb</scene>, resolution 2.40Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=A:ADENOSINE-5'-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=C:CYTIDINE-5'-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=G:GUANOSINE-5'-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=U:URIDINE-5'-MONOPHOSPHATE'>U</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Ribonuclease_H Ribonuclease H], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.4 3.1.26.4] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribonuclease_H Ribonuclease H], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.4 3.1.26.4] </span> | ||
|GENE= RNASEH1, RNH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= RNASEH1, RNH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2qk9|2QK9]], [[2qkk|2QKK]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qkb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qkb OCA], [http://www.ebi.ac.uk/pdbsum/2qkb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qkb RCSB]</span> | |||
}} | }} | ||
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[[Category: Nowotny, M.]] | [[Category: Nowotny, M.]] | ||
[[Category: Yang, W.]] | [[Category: Yang, W.]] | ||
[[Category: hydrolase/dna/rna complex]] | [[Category: hydrolase/dna/rna complex]] | ||
[[Category: | [[Category: rna/dna hybrid]] | ||
[[Category: rnase h]] | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:50:15 2008'' |
Revision as of 04:50, 31 March 2008
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, resolution 2.40Å | |||||||
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Ligands: | , , , , , , , , , , | ||||||
Gene: | RNASEH1, RNH1 (Homo sapiens) | ||||||
Activity: | Ribonuclease H, with EC number 3.1.26.4 | ||||||
Related: | 2QK9, 2QKK
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Human RNase H catalytic domain mutant D210N in complex with 20-mer RNA/DNA hybrid
OverviewOverview
We report here crystal structures of human RNase H1 complexed with an RNA/DNA substrate. Unlike B. halodurans RNase H1, human RNase H1 has a basic protrusion, which forms a DNA-binding channel and together with the conserved phosphate-binding pocket confers specificity for the B form and 2'-deoxy DNA. The RNA strand is recognized by four consecutive 2'-OH groups and cleaved by a two-metal ion mechanism. Although RNase H1 is overall positively charged, the substrate interface is neutral to acidic in character, which likely contributes to the catalytic specificity. Positions of the scissile phosphate and two catalytic metal ions are interdependent and highly coupled. Modeling of HIV reverse transcriptase (RT) with RNA/DNA in its RNase H active site suggests that the substrate cannot simultaneously occupy the polymerase active site and must undergo a conformational change to toggle between the two catalytic centers. The region that accommodates this conformational change offers a target to develop HIV-specific inhibitors.
About this StructureAbout this Structure
2QKB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structure of human RNase H1 complexed with an RNA/DNA hybrid: insight into HIV reverse transcription., Nowotny M, Gaidamakov SA, Ghirlando R, Cerritelli SM, Crouch RJ, Yang W, Mol Cell. 2007 Oct 26;28(2):264-76. PMID:17964265
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