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==Crystal structure of Q54A mutant protein of Bst-RNase HIII== | |||
<StructureSection load='3asm' size='340' side='right'caption='[[3asm]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3asm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ASM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ASM FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.603Å</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=3asm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3asm OCA], [https://pdbe.org/3asm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3asm RCSB], [https://www.ebi.ac.uk/pdbsum/3asm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3asm ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q6L6Q4_GEOSE Q6L6Q4_GEOSE] Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.[HAMAP-Rule:MF_00053][SAAS:SAAS00088233] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Ribonuclease H3 from Bacillus stearothermophilus (Bst-RNase H3) has the N-terminal TBP-like substrate-binding domain. To identify the substrate binding site in this domain, the mutant proteins of the intact protein and isolated N-domain, in which six of the seventeen residues corresponding to those involved in DNA binding of TBP are individually mutated to Ala, were constructed. All of them exhibited decreased enzymatic activities and/or substrate-binding affinities when compared to those of the parent proteins, suggesting that the N-terminal domain of RNase H3 uses the flat surface of the beta-sheet for substrate binding as TBP to bind DNA. This domain may greatly change conformation upon substrate binding. | |||
Identification of the substrate binding site in the N-terminal TBP-like domain of RNase H3.,Miyashita S, Tadokoro T, Angkawidjaja C, You DJ, Koga Y, Takano K, Kanaya S FEBS Lett. 2011 Jul 21;585(14):2313-7. Epub 2011 Jun 12. PMID:21664908<ref>PMID:21664908</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3asm" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Ribonuclease|Ribonuclease]] | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Geobacillus stearothermophilus]] | [[Category: Geobacillus stearothermophilus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Angkawidjaja | [[Category: Angkawidjaja C]] | ||
[[Category: Kanaya | [[Category: Kanaya S]] | ||
Latest revision as of 17:33, 1 November 2023
Crystal structure of Q54A mutant protein of Bst-RNase HIIICrystal structure of Q54A mutant protein of Bst-RNase HIII
Structural highlights
FunctionQ6L6Q4_GEOSE Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.[HAMAP-Rule:MF_00053][SAAS:SAAS00088233] Publication Abstract from PubMedRibonuclease H3 from Bacillus stearothermophilus (Bst-RNase H3) has the N-terminal TBP-like substrate-binding domain. To identify the substrate binding site in this domain, the mutant proteins of the intact protein and isolated N-domain, in which six of the seventeen residues corresponding to those involved in DNA binding of TBP are individually mutated to Ala, were constructed. All of them exhibited decreased enzymatic activities and/or substrate-binding affinities when compared to those of the parent proteins, suggesting that the N-terminal domain of RNase H3 uses the flat surface of the beta-sheet for substrate binding as TBP to bind DNA. This domain may greatly change conformation upon substrate binding. Identification of the substrate binding site in the N-terminal TBP-like domain of RNase H3.,Miyashita S, Tadokoro T, Angkawidjaja C, You DJ, Koga Y, Takano K, Kanaya S FEBS Lett. 2011 Jul 21;585(14):2313-7. Epub 2011 Jun 12. PMID:21664908[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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