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| | <StructureSection load='4z0u' size='340' side='right'caption='[[4z0u]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='4z0u' size='340' side='right'caption='[[4z0u]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4z0u]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco24 Eco24]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z0U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Z0U FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4z0u]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Escherichia_coli_O139:H28_str._E24377A Escherichia coli O139:H28 str. E24377A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z0U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z0U FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rnhA, EcE24377A_0219 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=331111 ECO24])</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=4z0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z0u OCA], [https://pdbe.org/4z0u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z0u RCSB], [https://www.ebi.ac.uk/pdbsum/4z0u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z0u ProSAT]</span></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>
| + | |
| - | <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=4z0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z0u OCA], [http://pdbe.org/4z0u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4z0u RCSB], [http://www.ebi.ac.uk/pdbsum/4z0u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4z0u ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RNH_ECO24 RNH_ECO24]] Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. | + | [https://www.uniprot.org/uniprot/RNH_ECO24 RNH_ECO24] Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. |
| | <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]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Eco24]] | + | [[Category: Escherichia coli]] |
| | + | [[Category: Escherichia coli O139:H28 str. E24377A]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ribonuclease H]]
| + | [[Category: Keck JL]] |
| - | [[Category: Keck, J L]] | + | [[Category: Petzold C]] |
| - | [[Category: Petzold, C]] | + | |
| - | [[Category: Hydrolase-peptide complex]]
| + | |
| - | [[Category: Peptide complex]]
| + | |
| - | [[Category: Ribonuclease]]
| + | |
| Structural highlights
Function
RNH_ECO24 Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Publication Abstract from PubMed
Single-stranded (ss) DNA-binding proteins (SSBs) bind and protect ssDNA intermediates formed during replication, recombination, and repair reactions. SSBs also directly interact with many different genome maintenance proteins to stimulate their enzymatic activities and/or mediate their proper cellular localization. We have identified an interaction formed between Escherichia coli SSB and ribonuclease HI (RNase HI), an enzyme that hydrolyzes RNA in RNA/DNA hybrids. The RNase HI.SSB complex forms by RNase HI binding the intrinsically disordered C terminus of SSB (SSB-Ct), a mode of interaction that is shared among all SSB interaction partners examined to date. Residues that comprise the SSB-Ct binding site are conserved among bacterial RNase HI enzymes, suggesting that RNase HI.SSB complexes are present in many bacterial species and that retaining the interaction is important for its cellular function. A steady-state kinetic analysis shows that interaction with SSB stimulates RNase HI activity by lowering the reaction Km. SSB or RNase HI protein variants that disrupt complex formation nullify this effect. Collectively our findings identify a direct RNase HI/SSB interaction that could play a role in targeting RNase HI activity to RNA/DNA hybrid substrates within the genome.
Interaction with Single-stranded DNA-binding Protein Stimulates Escherichia coli Ribonuclease HI Enzymatic Activity.,Petzold C, Marceau AH, Miller KH, Marqusee S, Keck JL J Biol Chem. 2015 Jun 5;290(23):14626-36. doi: 10.1074/jbc.M115.655134. Epub 2015, Apr 22. PMID:25903123[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Petzold C, Marceau AH, Miller KH, Marqusee S, Keck JL. Interaction with Single-stranded DNA-binding Protein Stimulates Escherichia coli Ribonuclease HI Enzymatic Activity. J Biol Chem. 2015 Jun 5;290(23):14626-36. doi: 10.1074/jbc.M115.655134. Epub 2015, Apr 22. PMID:25903123 doi:http://dx.doi.org/10.1074/jbc.M115.655134
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