Thioredoxin-like fold protein
WebNov 19, 2004 · We define the thioredoxin-like fold using the structure consensus of thioredoxin homologs and consider all circular permutations of the fold. The search for … WebMar 1, 1995 · The thioredoxin fold is a characteristic protein structural motif that has been found in five distinct classes of proteins that have the common property of interacting with cysteine-containing substrates. ... Cytochrome c biogenesis in a photosynthetic bacterium requires a periplasmic thioredoxin-like protein. Proc. Natl. Acad. Sci. USA, 90 ...
Thioredoxin-like fold protein
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WebApr 15, 2024 · We then used a combination of ELISA-based assay and purification strategies to show that deCoAlation is an enzyme-driven mechanism. Using mass-spectrometry and deCoAlation assays, we identified B. subtilis YtpP (thioredoxin-like protein) and thioredoxin A (TrxA) as enzymes that can remove CoA from different substrates. With mutagenesis … WebApr 28, 2014 · Thioredoxin-related protein of 14 kDa (TRP14, also called TXNDC17 for thioredoxin domain containing 17, or TXNL5 for thioredoxin-like 5) is an evolutionarily …
WebJun 25, 2015 · Fewer than 10 proteins are known to switch reversibly between distinct folds under native conditions, and they are collectively known as metamorphic proteins ( 20 ). KaiB is the only metamorphic protein known to function in biological clocks. Fig. 1 KaiB switches its fold to bind KaiC. WebThioredoxin - a fold for all reasons The thioredoxin fold is a characteristic protein structural motif that has been found in five distinct classes of proteins that have the common property of interacting with cysteine-containing substrates. Structure 15 March 1995, 3:245-250 The thioredoxin fold, named after the protein in which
Webdoxin-like fold. We employ this definition of the thioredoxin-like fold to query the PDB database using a protein structure motif search program (unpublished). Identified … WebJun 11, 2007 · The Dim protein family is composed of two classes, Dim1 and Dim2, which share a common thioredoxin-like fold. They were originally identified for their role in cell cycle progression and have been found to interact with Prp6, an essential component of the spliceosome, which forms the bridge of U4/U6.U5-tri-snRNP.
WebApr 15, 2024 · We then used a combination of ELISA-based assay and purification strategies to show that deCoAlation is an enzyme-driven mechanism. Using mass-spectrometry and …
WebJan 15, 2004 · Immunoglobulin-like fold; Immunoglobulin-like domain; Thioredoxin; Thioredoxin-like superfamily; Structure domains: V set domains (antibody variable domain-like) ... Prediction of residues in discontinuous B-cell epitopes using protein 3D structures. Haste Andersen et al. (2006) 10 more does social security card have middle nameWebApr 13, 2024 · HIGHLIGHTS. who: Sadek Amhaz from the (UNIVERSITY) have published the article: The UAS thioredoxin-like domain of UBXN7 regulates E3 ubiquitin ligase activity of RNF111/Arkadia, in the Journal: (JOURNAL) what: The authors have identified UBXN7 as a direct regulator of RNF111. Noticeably, the authors provide evidence that, unlike RNF111, … does social security back date disabilityWebOct 23, 2009 · Author Summary For any large class of proteins, far more protein sequences are known than can be examined experimentally. This is the case with the thioredoxin fold class, a large and diverse collection of proteins, some of which are known to catalyze important steps in metabolism. Some others participate in key processes like protein … face to face classes philippines advantageWebSusumu Imaoka, in International Review of Cell and Molecular Biology, 2011. 3.6 ERp18. ERp18 is the smallest member of the PDI family to contain a CXXC motif. Like the … does social security assist with burialThe thioredoxin fold is a protein fold common to enzymes that catalyze disulfide bond formation and isomerization. The fold is named for the canonical example thioredoxin and is found in both prokaryotic and eukaryotic proteins. It is an example of an alpha/beta protein fold that has oxidoreductase activity. The fold's spatial topology consists of a four-stranded antiparallel beta sheet sandwiched … does social security call your phoneWebStructure. Protein disulfide-isomerase has two catalytic thioredoxin-like domains (active sites), each containing the canonical CGHC motif, and two non catalytic domains. This structure is similar to the structure of enzymes responsible for oxidative folding in the intermembrane space of the mitochondria; an example of this is mitochondrial IMS import … face to face classes debateWebAll members of the PDI family share the thioredoxin-like domain structure characterized by the βαβαβαββα fold (Kemmink et al., 1997). PDI contains four thioredoxin-like domains abb'a'. The two redox active sites containing the CXXC motif are found in the a and a' domains (Figure 2). The active site domains are linked by the b and b ... face to face classes is better