ATP binding domain 4 Abstract: Difference between revisions

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ATP Binding Domain 4  
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.  
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)
//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
size, charge, chemical property of structure



Revision as of 06:51, 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 Archea. However the sequence similarity is very low compared to that for bacteria suggesting that bacteria is distantly related.