ArticleActa crystallographica. Section F, Structural biology communications2014
Characterization, crystallization and preliminary X-ray crystallographic analysis of the human Uba5 C-terminus-Ufc1 complex.
Article in Acta crystallographica. Section F, Structural biology communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- Allelic strengths of encephalopathy-associatedeLife · 2023Article
- A guide to UFMylation, an emerging posttranslational modification.The FEBS journal · 2023Review
- Review
- UFMylation System: An Emerging Player in Tumorigenesis.Cancers · 2022Review
- Structural basis for UFM1 transfer from UBA5 to UFC1.Nature communications · 2021Article
- A Concerted Action of UBA5 C-Terminal Unstructured Regions Is Important for Transfer of Activated UFM1 to UFC1.International journal of molecular sciences · 2021Article
- Highly Specialized Ubiquitin-Like Modifications: Shedding Light into the UFM1 Enigma.Biomolecules · 2021Review
- Decrypting UFMylation: How Proteins Are Modified with UFM1.Biomolecules · 2020Review
- Ubiquitin-like Protein Conjugation: Structures, Chemistry, and Mechanism.Chemical reviews · 2018Review
- Biallelic Variants in UBA5 Link Dysfunctional UFM1 Ubiquitin-like Modifier Pathway to Severe Infantile-Onset Encephalopathy.American journal of human genetics · 2016Article
- Structural and Functional Analysis of a Novel Interaction Motif within UFM1-activating Enzyme 5 (UBA5) Required for Binding to Ubiquitin-like Proteins and Ufmylation.The Journal of biological chemistry · 2016Article
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1 author at 1 institution in 1 country.
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Abstract
Human Uba5, which contains an adenylation domain and a C-terminal region, is the smallest ubiquitin-like molecule-activating enzyme. The mechanism through which the enzyme recognizes Ufc1 and catalyzes the formation of the Ufc1-Ufm1 complex remains unknown. In this study, Uba5 residues 364-404 were demonstrated to be necessary for the transthiolation of Ufm1 to Ufc1, and Uba5 381-404 was identified to be the minimal region for Ufc1 recognition. The fusion protein between Uba5 381-404 and Ufc1 was cloned, expressed and purified, and exists as a homodimer in solution. Crystallization was performed at 293 K using PEG 4000 as precipitant; the optimized crystals diffracted to 3.0 Å resolution and had unit-cell parameters a = b = 82.49, c = 62.47 Å, α = β = 90, γ = 120°. With one fusion-protein molecule in the asymmetric unit, the Matthews coefficient and solvent content were calculated to be 2.55 Å(3) Da(-1) and 51.84%, respectively.
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