1io2
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |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] | + | |ACTIVITY= <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> |
|GENE= RNHB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=311400 Thermococcus kodakarensis]) | |GENE= RNHB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=311400 Thermococcus kodakarensis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1io2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1io2 OCA], [http://www.ebi.ac.uk/pdbsum/1io2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1io2 RCSB]</span> | ||
}} | }} | ||
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[[Category: endonuclease]] | [[Category: endonuclease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:22:18 2008'' |
Revision as of 18:22, 30 March 2008
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| , resolution 2.00Å | |||||||
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| Gene: | RNHB (Thermococcus kodakarensis) | ||||||
| Activity: | Ribonuclease H, with EC number 3.1.26.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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