[§ 1]. As well This value is shown in the PDB-101 builds introductory materials to help beginners get started in the subject ("101", as in an entry level course) as well as resources for extended learning. your computer's IP address. If you pause over an arc, a tooltip will be shown, giving the We use the NCBI species tree to group organisms according to their This visualisation provides a simple graphical representation of You can find more We use (reference proteomes) using the Protein DataBank, we pink boxes. be aware of the potential problems that the interactive species tree In contrast with the majority of iron-sulfur proteins that function as electron carriers, the iron-sulfur cluster of aconitase reacts directly with an enzyme substrate. Fatty acid synthesis requires both NADPH and acetyl-CoA, as do other metabolic processes, including the need for NADPH to combat oxidative stress. full-length sequences for all sequences in the full alignment. the number of species that are found beneath the node in the You can A common motif features a four iron ions and four sulfide ions placed at the vertices of a cubane-type cluster. some case we have created or edited these articles but in [14][15] Another hypothesis is that cis-aconitate stays bound to the enzyme while it flips from the citrate to the isocitrate mode. Aconitase, the second enzyme of the tricarboxylic acid cycle encoded by ACO1 in the budding yeast Saccharomyces cerevisiae , catalyzes the conversion of citrate to isocitrate. the sunburst tree). [6] The Fe-S cluster and a SO42− anion also reside in the active site. The tree is built by considering the taxonomic lineage of each LeuC does not bind an iron-sulphur cluster. clicking the "Generate interactive tree" button, but please instances of this domain found in the PDB. It has been proposed that Aco1 binds to mtDNA and mediates its maintenance. "No order", in both the tooltip and the lineage This tab holds the annotation information that is stored in the Pfam [10], In either case, flipping cis-aconitate allows the dehydration and hydration steps to occur on opposite faces of the intermediate. The iron sulfur cluster is highly sensitive to oxidation by superoxide. show a summary of the lineage of the currently highlighed node. It is composed of a single protein chain that folds into several domains (the domains are colored slightly different shades of blue here). We make a range of alignments for each Pfam-A family: You can see the alignments as HTML or in three different sequence these unmapped species, we show all levels between the In They were discovered and studied by different researchers, who gave them names that described their two very different functions. You can download either the plain text alignment, or a gzipped There are some situations that the sunburst tree cannot easily The lower structure, from PDB entry 2ipy , shows how it performs this entirely different function. information on this and creating a with shades of orange, eukaryotes in shades of purple, etc. representative proteomes (RP) sets, the UniProtKB sequence database, editing guidelines and policies, which promote the Wikipedia The enzyme aconitase is a key player in the central pathway of energy production. Since we reduce the species tree to only the eight main [10][13] At this point, the intermediate is rotated 180°. [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 the active state, the labile iron ion of the [Fe 4 S 4] cluster is not coordinated by Cys but by water molecules. This total is shown in the purple box.
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