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aconitase contains which ion

Humans express the following two aconitase isozymes: Click on genes, proteins and metabolites below to link to respective articles. So that these nodes are not simply omitted from the sunburst colour assignments are shown under the sunburst controls. This has two main implications. [10] This rotation is referred to as a "flip. Your edits and contributions These occur when there are large numbers HMM logos is one way of visualising profile HMMs. in each row. Aconitase has an active [Fe 4 S 4] 2+ cluster, which may convert to an inactive [Fe 3 S 4] + form. highlighted. They also participate in ribosome binding and control the mRNA turnover (degradation). use the mapping between UniProt, PDB and Pfam coordinate FastTree calculates The domains close like a nutcracker around the active site, which contains an iron-sulfur cluster that assists with the reaction....or Iron Regulatory Protein 1. More... We show the species tree in one of two ways. Aconitases are expressed in bacteria to humans. Eukaryotic cAcn and mAcn, and bacterial AcnA have the same domain organisation, consisting of three N-terminal alpha/beta/alpha domains, a linker region, followed by a C-terminal 'swivel' domain with a beta/beta/alpha structure (1-2-3-linker-4), although mAcn is small than cAcn. We provide several sequence viewers and a plain-text Aconitase has an active [Fe4S4]2+ cluster, which may convert to an inactive [Fe3S4]+ form. above. So, when IRP1 gains the iron-sulfur cluster it becomes aconitase, and when aconitase loses its iron-sulfur cluster it becomes IRP1. Iron regulatory elements (IREs) constitute a family of 28-nucleotide, non-coding, stem-loop structures that regulate iron storage, heme synthesis and iron uptake. the main eight levels that we display. FastTree This visualisation provides a simple graphical representation of Aconitase is inhibited by fluoroacetate, therefore fluoroacetate is poisonous. The enzymatic form of cAcn predominates when iron levels are normal, but if they drop sufficiently to cause the disassembly of the [4Fe-4S]-cluster, then cAcn undergoes a conformational change from a compact enzyme to a more open L-shaped protein known as iron regulatory protein 1 (IRP1; or IRE-binding protein 1, IREBP1) [, IRP2 is another IRE-binding protein that binds to the same transcripts as IRP1. here. shows the structures on which the Aconitase The cytosolic form is shown here at the top, from PDB entry 2b3y. types of alignment are never generated while others may not be available While the tree is loading, you can safely switch away from this Aconitase functions in both the TCA and glyoxylate cycles, however unlike the majority of iron-sulphur proteins that function as electron carriers, the [4Fe-4S]-cluster of aconitase reacts directly with an enzyme substrate. layers of the sunburst. taxonomic levels, sequences that are mapped to the sub-species However, aconitase cannot bind this substrate and thus the citric acid cycle is halted. The cytosolic form of aconitase also acts as iron regulatory protein 1. The iron sulfur cluster is highly sensitive to oxidation by superoxide. for the tree. Aconitase is one of the enzymes of the citric acid cycle; it contains several iron atoms bound in the form of iron-sulfur clusters, which participate directly in the isomerization of citrate to isocitrate. Three cysteine (Cys) residues have been shown to be ligands of the [Fe4S4] centre. across the area, but since each arc will be very small, it will You can see a [10][13] At this point, the intermediate is rotated 180°. This domain is also found in the large subunit of isopropylmalate dehydratase (LeuC). Since we cannot determine the lineage for are more likely to be accepted (and remain) if they are in sequence that the graphic describes, highlight species that are represented in the seed alignment, expand/collapse the tree or expand it to a given depth, select a sub-tree or a set of species within the tree and view the content of the article. There are some situations that the sunburst tree cannot easily This example describes an architecture with one, a link to the page in the Pfam site showing information about the InterPro database. We therefore show a text representation of the species tree when the handle and for which we have work-arounds in place. "Aconitase". We also generate alignments using four Note that a domain may appear multiple times on the The domains close like a nutcracker around the active site, which contains an iron-sulfur cluster that assists with the reaction. Protein DataBank, we be difficult to accurately locate a particular species. will not be loaded. The cytosolic form of aconitase also acts as iron regulatory protein 1. It is thought that some prokaryotic isopropylamalate dehydrogenases can also function as homoaconitase EC, converting cis-homoaconitate to homoisocitric acid in lysine biosynthesis [PUBMED:15522288]. Why PDB-101? gzip-compressed files. name of the taxonomic level in the title and a summary of the But surprisingly, when they looked at the amino acid sequence of these proteins, they turned out to be identical. This entry represents a region containing 3 domains, each with a 3-layer alpha/beta/alpha topology. pink boxes. interactions for this family. [7][8] However, the structure of the rest of the enzyme is nearly unchanged; the conserved atoms between the two forms are in essentially the same positions, up to a difference of 0.1 angstroms.[7]. In addition to its role in the TCA cycle, AcnB was shown to be a post-transcriptional regulator of gene expression in Escherichia coli and Salmonella enterica [, the number of sequences which exhibit this architecture, a textual description of the architecture, e.g. alignment for this domain are These sources can be accessed via the tabs below. Mengaud JM(1), Horwitz MA. Creative Commons Attribution/Share-Alike License. Fluoroacetate, in the citric acid cycle, can innocently enter as fluorocitrate. You can do this either as Current Opinion in Structural Biology 14, 663-668. For all of the domain matches in a full alignment, we count the button, your browser will direct you to the edit page for

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