1io2

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[[Image:1io2.jpg|left|200px]]<br /><applet load="1io2" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1io2.jpg|left|200px]]
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caption="1io2, resolution 2.00&Aring;" />
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'''CRYSTAL STRUCTURE OF TYPE 2 RIBONUCLEASE H FROM HYPERTHERMOPHILIC ARCHAEON, THERMOCOCCUS KODAKARAENSIS KOD1'''<br />
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{{Structure
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|PDB= 1io2 |SIZE=350|CAPTION= <scene name='initialview01'>1io2</scene>, resolution 2.00&Aring;
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|SITE=
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|LIGAND=
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|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]
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|GENE= RNHB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=311400 Thermococcus kodakarensis])
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}}
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'''CRYSTAL STRUCTURE OF TYPE 2 RIBONUCLEASE H FROM HYPERTHERMOPHILIC ARCHAEON, THERMOCOCCUS KODAKARAENSIS KOD1'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1IO2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermococcus_kodakarensis Thermococcus kodakarensis]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IO2 OCA].
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1IO2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermococcus_kodakarensis Thermococcus kodakarensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IO2 OCA].
==Reference==
==Reference==
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Catalytic center of an archaeal type 2 ribonuclease H as revealed by X-ray crystallographic and mutational analyses., Muroya A, Tsuchiya D, Ishikawa M, Haruki M, Morikawa M, Kanaya S, Morikawa K, Protein Sci. 2001 Apr;10(4):707-14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11274461 11274461]
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Catalytic center of an archaeal type 2 ribonuclease H as revealed by X-ray crystallographic and mutational analyses., Muroya A, Tsuchiya D, Ishikawa M, Haruki M, Morikawa M, Kanaya S, Morikawa K, Protein Sci. 2001 Apr;10(4):707-14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11274461 11274461]
[[Category: Ribonuclease H]]
[[Category: Ribonuclease H]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: endonuclease]]
[[Category: endonuclease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:52:46 2008''

Revision as of 09:52, 20 March 2008


PDB ID 1io2

Drag the structure with the mouse to rotate
, resolution 2.00Å
Gene: RNHB (Thermococcus kodakarensis)
Activity: Ribonuclease H, with EC number 3.1.26.4
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF TYPE 2 RIBONUCLEASE H FROM HYPERTHERMOPHILIC ARCHAEON, THERMOCOCCUS KODAKARAENSIS KOD1


Overview

The catalytic center of an archaeal Type 2 RNase H has been identified by a combination of X-ray crystallographic and mutational analyses. The crystal structure of the Type 2 RNase H from Thermococcus kodakaraensis KOD1 has revealed that the N-terminal major domain adopts the RNase H fold, despite the poor sequence similarity to the Type 1 RNase H. Mutational analyses showed that the catalytic reaction requires four acidic residues, which are well conserved in the Type 1 RNase H and the members of the polynucleotidyl transferase family. Thus, the Type 1 and Type 2 RNases H seem to share a common catalytic mechanism, except for the requirement of histidine as a general base in the former enzyme. Combined with the results from deletion mutant analyses, the structure suggests that the C-terminal domain of the Type 2 RNase H is involved in the interaction with the DNA/RNA hybrid.

About this Structure

1IO2 is a Single protein structure of sequence from Thermococcus kodakarensis. Full crystallographic information is available from OCA.

Reference

Catalytic center of an archaeal type 2 ribonuclease H as revealed by X-ray crystallographic and mutational analyses., Muroya A, Tsuchiya D, Ishikawa M, Haruki M, Morikawa M, Kanaya S, Morikawa K, Protein Sci. 2001 Apr;10(4):707-14. PMID:11274461

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