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3u3g

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[[Image:3u3g.png|left|200px]]
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==Structure of LC11-RNase H1 Isolated from Compost by Metagenomic Approach: Insight into the Structural Bases for Unusual Enzymatic Properties of Sto-RNase H1==
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<StructureSection load='3u3g' size='340' side='right' caption='[[3u3g]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3u3g]] 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=3U3G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U3G FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene></td></tr>
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<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>
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<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=3u3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u3g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u3g RCSB], [http://www.ebi.ac.uk/pdbsum/3u3g PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Metagenome-derived LC11-RNase H1 is a homolog of Sulfolobus tokodaii RNase H1 (Sto-RNase H1). It lacks a C-terminal tail, which is responsible for hyperstabilization of Sto-RNase H1. Sto-RNase H1 is characterized by its ability to cleave not only an RNA/DNA hybrid but also a double-stranded RNA (dsRNA). To examine whether LC11-RNase H1 also exhibits both RNase H and dsRNase activities, LC11-RNase H1 was overproduced in Escherichia coli, purified, and characterized. LC11-RNase H1 exhibited RNase H activity with similar metal ion preference, optimum pH, and cleavage mode of substrate with those of Sto-RNase H1. However, LC11-RNase H1 did not exhibit dsRNase activity at any condition examined. LC11-RNase H1 was less stable than Sto-RNases H1 and its derivative lacking the C-terminal tail (Sto-RNase H1DeltaC6) by 37 and 13 degrees C in T(m) , respectively. To understand the structural bases for these differences, the crystal structure of LC11-RNase H1 was determined at 1.4 A resolution. The LC11-RNase H1 structure is highly similar to the Sto-RNase H1 structure. However, LC11-RNase H1 has two grooves on protein surface, one containing the active site and the other containing DNA-phosphate binding pocket, while Sto-RNase H1 has one groove containing the active site. In addition, LC11-RNase H1 contains more cavities and buried charged residues than Sto-RNase H1. We propose that LC11-RNase H1 does not exhibit dsRNase activity because dsRNA cannot fit to the two grooves on protein surface and that LC11-RNase H1 is less stable than Sto-RNase H1DeltaC6 because of the increase in cavity volume and number of buried charged residues.
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{{STRUCTURE_3u3g| PDB=3u3g | SCENE= }}
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Activity, stability, and structure of metagenome-derived LC11-RNase H1, a homolog of Sulfolobus tokodaii RNase H1.,Nguyen TN, Angkawidjaja C, Kanaya E, Koga Y, Takano K, Kanaya S Protein Sci. 2012 Apr;21(4):553-61. doi: 10.1002/pro.2043. Epub 2012 Mar 2. PMID:22389131<ref>PMID:22389131</ref>
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===Structure of LC11-RNase H1 Isolated from Compost by Metagenomic Approach: Insight into the Structural Bases for Unusual Enzymatic Properties of Sto-RNase H1===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_22389131}}
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==About this Structure==
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[[3u3g]] 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=3U3G OCA].
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==See Also==
==See Also==
*[[Ribonuclease|Ribonuclease]]
*[[Ribonuclease|Ribonuclease]]
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*[[User:Jaime.Prilusky/Test/tree|User:Jaime.Prilusky/Test/tree]]
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==Reference==
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== References ==
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<ref group="xtra">PMID:022389131</ref><references group="xtra"/>
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<references/>
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__TOC__
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</StructureSection>
[[Category: Ribonuclease H]]
[[Category: Ribonuclease H]]
[[Category: Uncultured organism]]
[[Category: Uncultured organism]]
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[[Category: Angkawidjaja, C.]]
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[[Category: Angkawidjaja, C]]
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[[Category: Kanaya, E.]]
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[[Category: Kanaya, E]]
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[[Category: Kanaya, S.]]
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[[Category: Kanaya, S]]
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[[Category: Koga, Y.]]
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[[Category: Koga, Y]]
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[[Category: Nguyen, T N.]]
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[[Category: Nguyen, T N]]
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[[Category: Takano, K.]]
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[[Category: Takano, K]]
[[Category: Cleave the rna strand of rna/dna hybrid]]
[[Category: Cleave the rna strand of rna/dna hybrid]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]

Revision as of 15:53, 9 December 2014

Structure of LC11-RNase H1 Isolated from Compost by Metagenomic Approach: Insight into the Structural Bases for Unusual Enzymatic Properties of Sto-RNase H1

3u3g, resolution 1.40Å

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