0000000000760116

AUTHOR

Janis Rumnieks

showing 4 related works from this author

Bacterial Viruses Subcommittee and Archaeal Viruses Subcommittee of the ICTV: Update of taxonomy changes in 2021

2021

In this article, we – the Bacterial Viruses Subcommittee and the Archaeal Viruses Subcommittee of the International Committee on Taxonomy of Viruses (ICTV) – summarise the results of our activities for the period March 2020 – March 2021. We report the division of the former Bacterial and Archaeal Viruses Subcommittee in two separate Subcommittees, welcome new members, a new Subcommittee Chair and Vice Chair, and give an overview of the new taxa that were proposed in 2020, approved by the Executive Committee and ratified by vote in 2021. In particular, a new realm, three orders, 15 families, 31 subfamilies, 734 genera and 1845 species were newly created or redefined (moved/promoted). Supplem…

Archaeal VirusesSocieties ScientificviruksetLibrary scienceBiologybakteriofagitExecutive committee03 medical and health sciencesVirology Division NewsVirologyvirusesBacteriophages030304 developmental biologyTaxonomy11832 Microbiology and virology0303 health sciencesScience & TechnologyBacteria030306 microbiologysystematiikka (biologia)Archaeal VirusesGeneral MedicineArchaeaVirologyvirologia[SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/VirologyTaxonomy (biology)Bacterial virusLife Sciences & Biomedicine
researchProduct

Crystal structure of human gamma-butyrobetaine hydroxylase.

2010

Gamma-butyrobetaine hydroxylase (GBBH) is a 2-ketoglutarate-dependent dioxygenase that catalyzes the biosynthesis of l-carnitine by hydroxylation of gamma-butyrobetaine (GBB). l-carnitine is required for the transport of long-chain fatty acids into mitochondria for generating metabolic energy. The only known synthetic inhibitor of GBBH is mildronate (3-(2,2,2-trimethylhydrazinium) propionate dihydrate), which is a non-hydroxylatable analog of GBB. To aid in the discovery of novel GBBH inhibitors by rational drug design, we have solved the three-dimensional structure of recombinant human GBBH at 2.0A resolution. The GBBH monomer consists of a catalytic double-stranded beta-helix (DBSH) domai…

EGF-like domainStereochemistrygamma-Butyrobetaine DioxygenaseBiophysicsDrug designBiochemistryHydroxylationchemistry.chemical_compoundDioxygenaseCatalytic DomainHumansEnzyme InhibitorsMolecular BiologyHistidinechemistry.chemical_classificationCrystallographybiologyActive siteCell BiologyRecombinant ProteinsZincEnzymeBiochemistrychemistryCyclic nucleotide-binding domainDrug Designbiology.proteinProtein MultimerizationMethylhydrazinesBiochemical and biophysical research communications
researchProduct

Crystal Structure of the Maturation Protein from Bacteriophage Qβ

2017

Abstract Virions of the single-stranded RNA bacteriophages contain a single copy of the maturation protein, which is bound to the phage genome and is required for the infectivity of the particles. The maturation protein mediates the adsorption of the virion to bacterial pili and the subsequent release and penetration of the genome into the host cell. Here, we report a crystal structure of the maturation protein from bacteriophage Qβ. The protein has a bent, highly asymmetric shape and spans 110 A in length. Apart from small local substructures, the overall fold of the maturation protein does not resemble that of other known proteins. The protein is organized in two distinct regions, an α-he…

Gene Expression Regulation Viral0301 basic medicineVesicle-associated membrane protein 8Protein ConformationRNA-binding proteinRNA PhagesPilus03 medical and health sciencesStructural BiologyBacteriophagesAmino Acid SequenceCloning MolecularMolecular Biology030102 biochemistry & molecular biologybiologyCryoelectron MicroscopyVirionRNA Phagesbiology.organism_classificationMolecular biologyProtein tertiary structureCell biology030104 developmental biologyCapsidbiology.proteinRNA ViralCapsid ProteinsProtein GBacteriophage QβJournal of Molecular Biology
researchProduct

Structure of AP205 Coat Protein Reveals Circular Permutation in ssRNA Bacteriophages.

2016

We are thankful to the MAX-lab staff for their support during our visit at the synchrotron.; International audience; AP205 is a single-stranded RNA bacteriophage that has a coat protein sequence not similar to any other known single-stranded RNA phage. Here, we report an atomic-resolution model of the AP205 virus-like particle based on a crystal structure of an unassembled coat protein dimer and a cryo-electron microscopy reconstruction of the assembled particle, together with secondary structure information from site-specific solid-state NMR data. The AP205 coat protein dimer adopts the conserved Leviviridae coat protein fold except for the N-terminal region, which forms a beta-hairpin in …

0301 basic medicineModels MolecularRNA bacteriophageViral proteinCryo-electron microscopyProtein Conformation010402 general chemistrymedicine.disease_causeCrystallography X-Ray01 natural sciencesvirus-like particleBacteriophage03 medical and health sciencesStructural Biology[CHIM.ANAL]Chemical Sciences/Analytical chemistryLeviviridaemedicineRNA VirusesBacteriophages[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]Molecular BiologyProtein secondary structurebiologyCryoelectron MicroscopyRNA[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologycircular permutationRNA PhagesCircular permutation in proteinsbiology.organism_classification3. Good health0104 chemical sciencesCrystallography030104 developmental biologycoat proteinBiophysicsLeviviridaeCapsid ProteinsJournal of molecular biology
researchProduct