ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010
Structure of an essential bacterial protein YeaZ (TM0874) from Thermotoga maritima at 2.5 Å resolution.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 19 citations in OpenAlex.
- New Insights into the Biological Functions of Essential TsaB/YeaZ Protein inAntibiotics (Basel, Switzerland) · 2024Article
- Conservation and Diversification of tRNA tInternational journal of molecular sciences · 2022Review
- Conformational communication mediates the reset step in t6A biosynthesis.Nucleic acids research · 2019Article
- The structure of the TsaB/TsaD/TsaE complex reveals an unexpected mechanism for the bacterial t6A tRNA-modification.Nucleic acids research · 2018Article
- Structure and mechanism of a bacterial t6A biosynthesis system.Nucleic acids research · 2018Article
- The ATP-mediated formation of the YgjD-YeaZ-YjeE complex is required for the biosynthesis of tRNA t6A in Escherichia coli.Nucleic acids research · 2015Article
- Determination of essentiality and regulatory function of staphylococcal YeaZ in branched-chain amino acid biosynthesis.Virulence · 2015Article
- Structural updates of alignment of protein domains and consequences on evolutionary models of domain superfamilies.BioData mining · 2013Article
- Crystal structure of the dimer of two essential Salmonella typhimurium proteins, YgjD & YeaZ and calorimetric evidence for the formation of a ternary YgjD-YeaZ-YjeE complex.Protein science : a publication of the Protein Society · 2013Article
- A role for the universal Kae1/Qri7/YgjD (COG0533) family in tRNA modification.The EMBO journal · 2011Article
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Authors and funding
34 authors at 7 institutions in 1 country.
Funding
Abstract
YeaZ is involved in a protein network that is essential for bacteria. The crystal structure of YeaZ from Thermotoga maritima was determined to 2.5 Å resolution. Although this protein belongs to a family of ancient actin-like ATPases, it appears that it has lost the ability to bind ATP since it lacks some key structural features that are important for interaction with ATP. A conserved surface was identified, supporting its role in the formation of protein complexes.
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