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| | <StructureSection load='4h8k' size='340' side='right'caption='[[4h8k]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='4h8k' size='340' side='right'caption='[[4h8k]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4h8k]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Uncultured_organism Uncultured organism]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H8K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4H8K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4h8k]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Uncultured_organism Uncultured organism]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H8K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H8K FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4h8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h8k OCA], [https://pdbe.org/4h8k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h8k RCSB], [https://www.ebi.ac.uk/pdbsum/4h8k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h8k ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4h8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h8k OCA], [http://pdbe.org/4h8k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4h8k RCSB], [http://www.ebi.ac.uk/pdbsum/4h8k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4h8k ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/E0X767_9ZZZZ E0X767_9ZZZZ] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Ribonuclease|Ribonuclease]] | + | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] |
| - | *[[Temp|Temp]]
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ribonuclease H]] | |
| | [[Category: Uncultured organism]] | | [[Category: Uncultured organism]] |
| - | [[Category: Kanaya, E]] | + | [[Category: Kanaya E]] |
| - | [[Category: Kanaya, S]] | + | [[Category: Kanaya S]] |
| - | [[Category: Matsumoto, H]] | + | [[Category: Matsumoto H]] |
| - | [[Category: Nguyen, T N]] | + | [[Category: Nguyen TN]] |
| - | [[Category: You, D J]] | + | [[Category: You DJ]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Hydrolase-dna-rna complex]]
| + | |
| - | [[Category: Ribonuclease h]]
| + | |
| - | [[Category: Ribonuclease h rna dna hybrid]]
| + | |
| - | [[Category: Rnase h]]
| + | |
| Structural highlights
Function
E0X767_9ZZZZ
Publication Abstract from PubMed
LC11-RNase H1 is a Sulfolobus tokodaii RNase H1 (Sto-RNase H1) homologue isolated by metagenomic approach. In this study, the crystal structure of LC11-RNase H1 in complex with an RNA/DNA substrate was determined. Unlike Bacillus halodurans RNase H1 without hybrid binding domain (HBD) (Bh-RNase HC) and human RNase H1 without HBD (Hs-RNase HC), LC11-RNase H1 interacts with four non-consecutive 2'-OH groups of the RNA strand. The lack of interactions with four consecutive 2'-OH groups leads to a dramatic decrease in the ability of LC11-RNase H1 to cleave the DNA-RNA-DNA/DNA substrate containing four ribonucleotides as compared to those to cleave the substrates containing five and six ribonucleotides. The interaction of LC11-RNase H1 with the DNA strand is also different from those of Bh-RNase HC and Hs-RNase HC. Beside the common phosphate-binding pocket, LC11-RNase H1 has a unique DNA-binding channel. Furthermore, the active-site residues of LC11-RNase H1 are located farther away from the scissile phosphate group than those of Bh-RNase HC and Hs-RNase HC. Modeling of Sto-RNase H1 in complex with the 14bp RNA/DNA substrate, together with the structure-based mutational analyses, suggest that the ability of Sto-RNase H1 to cleave double-stranded RNA is dependent on the local conformation of the basic residues located at the DNA binding site.
Crystal structure of metagenome-derived LC11-RNase H1 in complex with RNA/DNA hybrid.,Nguyen TN, You DJ, Matsumoto H, Kanaya E, Koga Y, Kanaya S J Struct Biol. 2013 May;182(2):144-54. doi: 10.1016/j.jsb.2013.02.018. Epub 2013 , Mar 14. PMID:23500886[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nguyen TN, You DJ, Matsumoto H, Kanaya E, Koga Y, Kanaya S. Crystal structure of metagenome-derived LC11-RNase H1 in complex with RNA/DNA hybrid. J Struct Biol. 2013 May;182(2):144-54. doi: 10.1016/j.jsb.2013.02.018. Epub 2013 , Mar 14. PMID:23500886 doi:10.1016/j.jsb.2013.02.018
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