1io2: Difference between revisions
New page: left|200px<br /><applet load="1io2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1io2, resolution 2.00Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:1io2.jpg|left|200px]]<br /><applet load="1io2" size=" | [[Image:1io2.jpg|left|200px]]<br /><applet load="1io2" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1io2, resolution 2.00Å" /> | caption="1io2, resolution 2.00Å" /> | ||
'''CRYSTAL STRUCTURE OF TYPE 2 RIBONUCLEASE H FROM HYPERTHERMOPHILIC ARCHAEON, THERMOCOCCUS KODAKARAENSIS KOD1'''<br /> | '''CRYSTAL STRUCTURE OF TYPE 2 RIBONUCLEASE H FROM HYPERTHERMOPHILIC ARCHAEON, THERMOCOCCUS KODAKARAENSIS KOD1'''<br /> | ||
==Overview== | ==Overview== | ||
The catalytic center of an archaeal Type 2 RNase H has been identified by | 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== | ==About this Structure== | ||
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:// | 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]. | ||
==Reference== | ==Reference== | ||
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[[Category: endonuclease]] | [[Category: endonuclease]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:48 2008'' | ||
Revision as of 11:13, 21 February 2008
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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. Active as Ribonuclease H, with EC number 3.1.26.4 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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