1ril

CRYSTAL STRUCTURE OF RIBONUCLEASE H FROM THERMUS THERMOPHILUS HB8 REFINED AT 2.8 ANGSTROMS RESOLUTIONCRYSTAL STRUCTURE OF RIBONUCLEASE H FROM THERMUS THERMOPHILUS HB8 REFINED AT 2.8 ANGSTROMS RESOLUTION

Structural highlights 1ril is a 1 chain structure with sequence from Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Activity: Ribonuclease H, with EC number 3.1.26.4 Resources: FirstGlance, OCA, RCSB, PDBsum Function [RNH_THET8] Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The crystal structure of Thermus thermophilus RNase H was determined at 2.8 A resolution. The structure was solved by the molecular replacement method, based on the accurately refined structure of Escherichia coli RNase HI, which shows 52% amino acid sequence identity. Crystallographic refinement led to an R-factor of 0.205, with a 0.019 A root-mean-square deviation from ideal bond lengths and 0.048 A from ideal bond angle distances. Structural comparison shows a striking similarity in the overall folding of the thermophilic and mesophilic enzymes. The root-mean-square displacement is 0.95 A between equivalent alpha-carbon atoms from all elements of secondary structure (five alpha-helices and five beta-strands). However, some notable differences, which account for the enhanced thermostability of T. thermophilus RNase H, are observed in loop structures and side-chain conformations. The substitution of Gly for the left-handed helical residue (Lys95) in the E. coli enzyme is proposed to substantially enhance the thermostability, due to the release of steric hindrance caused by the beta-carbon atom. Furthermore, it is likely that the expansion of an aromatic cluster, arising from the replacement of Ile78 in the mesophilic enzyme by Phe, and the increased number of salt-bridges additively contribute to the stability. Crystal structure of ribonuclease H from Thermus thermophilus HB8 refined at 2.8 A resolution.,Ishikawa K, Okumura M, Katayanagi K, Kimura S, Kanaya S, Nakamura H, Morikawa K J Mol Biol. 1993 Mar 20;230(2):529-42. PMID:8385228 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribonuclease Temp User:Jaime.Prilusky/Test/tree

spinqualitylabelsall models 1ril, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image