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Gloydius rubromaculatus

ABSTRACT: Gloydius rubromaculatus overview

PROVIDER: PRJNA848905 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR14235847_1.fastq.gz	Fastqsanger.gz
	SRR14235847_2.fastq.gz	Fastqsanger.gz

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Structure of saxthrombin, a thrombin-like enzyme from Gloydius saxatilis.

Project description:Snake-venom thrombin-like enzymes (SVTLEs) are serine proteases that are widely distributed in snakes from the Crotalinae subfamily of the Viperidae. In contrast to other snake-venom serine proteases, they have a biochemical activity similar to that of thrombin and play an important role in the process of blood coagulation. However, SVTLEs cannot activate factor VIII, which is essential in blood-clot stabilization. Consequently, blood clots produced by SVTLEs are not stable and are cleared rapidly. This characteristic makes SVTLEs attractive as potential candidates for antithrombotic therapy. Saxthrombin, an SVTLE from Gloydius saxatilis, was purified and crystallized to obtain a high-quality crystal, from which data were acquired to 1.43?Å resolution. Preliminary X-ray diffraction analysis showed that the crystal belonged to space group C2, with unit-cell parameters a = 94.2, b = 52.2, c = 50.1?Å, ? = 96.7°. The crystal structure was determined by molecular replacement and the final R factor was 18.69%; the R(free) was 20.01%. This is the first report of a crystal structure of an SVTLE. Saxthrombin belongs to the typical ?/?-hydrolase fold of serine proteases. Its structure was compared with those of thrombin and other snake-venom serine proteases. The observed differences in the amino-acid composition of the loops surrounding the active site appear to contribute to different surface-charge distributions and thus alter the shape of the active-site cleft, which may explain the differences in substrate affinity.

| S-EPMC3151115 | biostudies-literature

Complete mitochondrial genome of <i>Gloydius saxatilis</i> (Viperidae: Crotalinae) from Korea.

Project description:In this study, we sequenced the complete mitochondrial genome of Gloydius saxatilis using Illumina next-generation sequencing. The total length of the mitogenome was 17,223 bp, and contained 13 protein-coding genes (PCGs), two ribosomal RNAs (rRNAs), 22 transfer RNAs (tRNAs), two non-coding control regions (CRs), and the origin of light (OL)-strand replication. The genome structure and order of the genes were similar to other Crotalinae species. Phylogenetic analysis based on the 13 concatenated PCGs indicated that G. saxatilis closely related to G. intermedius and, G. shedaoensis.

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Project description:Gloydius shedaoensis raw ddRAD sequence reads

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Qualitative Analysis of Proteins in Two Snake Venoms, Gloydius Blomhoffii and Agkistrodon Acutus.

Project description:ObjectivesSnake venom is a complex mixture of various pharmacologically active substances, such as small proteins, peptides, and organic and mineral components. This paper aims to identify and analyse the proteins in common venomous snakes, such as Gloydius blomhoffii (G. blomhoffii) and Agkistrodon acutus (A. acutus), in Korea.MethodsWe used mass spectrometry, electrophoresis, N-terminal sequencing and in-gel digestion to analyse the proteins in these two snake venoms.ResultsWe identified eight proteins in G. blomhoffii venom and four proteins in A. acutus venom. The proteins detected in G. blomhoffii and A. acutus venoms were phospholipase A2, snake venom metalloproteinase and cysteine-rich secretory protein. Snake C-type lectin (snaclec) was unique to A. acutus venom.ConclusionThese data will contribute to the current knowledge of proteins present in the venoms of viper snakes and provide useful information for investigating their therapeutic potential.

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