ATP binding domain 4 Abstract: Difference between revisions
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Multiple sequence alignment revealed three significant conserved residues which are identified as PP-loop motif. This motif is conserved across species in Eukarya and Archaea. However the sequence similarity is very low compared to that for bacteria suggesting that bacteria is distantly related. This evolutionary relationship between species can be observed on phylogenetic tree that was constructed. | Multiple sequence alignment revealed three significant conserved residues which are identified as PP-loop motif. This motif is conserved across species in Eukarya and Archaea. However the sequence similarity is very low compared to that for bacteria suggesting that bacteria is distantly related. This evolutionary relationship between species can be observed on phylogenetic tree that was constructed. | ||
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Revision as of 11:17, 5 June 2009
ATP Binding Domain 4 Two high z score proteins, arginosuccinate synthase and quesosine biosynthesis, were selected through Dali analysis. Structural alignment and comparison based on cleft volume and superimposed structures by PyMOL revealed that arginosuccinate synthase was the most similar to ATP binding domain 4. //function of arginosuccinate synthase is for ATP hydrolysis (do not mention citrulline, like making a particular residue -ve to facilitate ATP cleavage) size, charge, chemical property of structure
Domain A is in close proximity to ATP whereas domain B may not participate in ATP recognition or involved in other substrate interactions.
Multiple sequence alignment revealed three significant conserved residues which are identified as PP-loop motif. This motif is conserved across species in Eukarya and Archaea. However the sequence similarity is very low compared to that for bacteria suggesting that bacteria is distantly related. This evolutionary relationship between species can be observed on phylogenetic tree that was constructed.
