pyrococcus furiosus domain

To the best of our knowledge, no Pyrococcus furiosus proteins have so far been shown to have domain-specific chaperone activity. The crystal structure of the catalytic domain of a chitinase from the hyperthermophilic archaeon Pyrococcus furiosus (AD2 PF-ChiA) has been determined at 1.5 Å resolution.This is the first structure of the catalytic domain of an archaeal chitinase. Here, we report the crystal structure of the helicase domain of the Hef protein from Pyrococcus furiosus. Divergence of the hyperthermophilic Archaea, Pyrococcus furiosus and Pyrococcus horikoshii, was assessed by analysis of complete genomic sequences of both species. We have discovered an unusual processing pathway of pre-rRNA in extreme thermophilic archaea exemplified by Pyrococcus furiosus. Genome structure. In Pyrococcus furiosus, the transcriptional regulator CopR is encoded by the gene pf0739, which is in divergent orientation to copA (pf0740). STRUCTURE NOTE Structural Genomics of Pyrococcus furiosus: X-Ray Crystallography Reveals 3D Domain Swapping in Rubrerythrin Wolfram Tempel, 1Zhi-Jie (James) Liu, Florian D. Schubot, Ashit Shah,1 Michael V. Weinberg,1 Francis E. Jenney, Jr.,1 W. Bryan Arendall, III, 2Michael W. W. Adams,1 Jane S. Richardson, David C. Richardson,2 John P. Rose, 1* and Bi … Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) Status. This chitinase has unique structural features; it contains two catalytic domains (AD1 and AD2) and two … Yet, provocative variations to the general schemes exist. [citation needed] The genomes encode for many different metabolic enzymes which gives themselves a wider spectrum of living conditions because they can transport and metabolize a wide range of … Synthesis and assembly of ribosomal components are fundamental cellular processes and generally well-conserved within the main groups of organisms. The aim of this study was to analyze in vivo if the one nucleotide insertion is responsible for the inability to grow on chitin, using a recently described genetic system for Pyrococcus furiosus. From these data we assume that Pyrococcus furiosus is most likely unable to use chitin as a carbon source. The average nucleotide identity between the genomic sequences is 70–75% within ORFs. Here, we report the crystal structure of the helicase domain of the Hef protein from Pyrococcus furiosus. This positively charged extra region, structurally similar to the "thumb" domain of DNA polymerase, plays critical roles in fork recognition. A chitinase, from Pyrococcus furiosus, is a hyperthermophilic glycosidase that effectively hydrolyses both α and β crystalline chitin. Reviewed-Annotation score: ... Family and domain databases. The archaeal Hef helicase/ nuclease is a representative protein that processes flap- or fork-DNA structures, and, intriguingly, its C-terminal half belongs to the XPF/Mus81 nuclease family. Here we report that the N-terminal domain of Pyrococcus furiosus L-asparaginase, (NPfA, a protein chaperone lacking α-crystallin domain) can serve as … Three of the Pyrococcus species have been sequenced.P. Pyrococcus furiosus Vc 1 is an anaerobe, hyperthermophilic archaeon that was isolated from geothermally heated marine sediment.. anaerobe; hyperthermophilic; 16S sequence; Archaea; genome sequence The P. furiosus genome (1.908 mbp) is 170 kbp larger than The structure reveals a novel helical insertion between the two conserved helicase core domains. Results Protein purificationAfter affinity chromatography, refolding and centrifugation, the majority of the NPfA appeared in the soluble fraction which showed a single 22 kDa band on SDS/PAGE. furiosus is the largest containing 1.9Mb followed by P. abyssi with 1.8Mb and P. horikoshii with 1.7Mb.

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