3bsqA Discussion: Difference between revisions

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'''Multiple sequence alighment''' (MSA) revealed some conserved residues throughput the whole sulfatase family. Previous experiemnts on catalytic activity of sulfatases describe a set of residues which are essential for the function of sulfatases. A histidine residue (H)  and two or more '''''sequential''''' arganine residues (R) are known to be essential, and also characteristic of the N-terminal active site of sulfatases. Our MSA resultaed a number of residues conserves in the N-terminus, along with a H and one R residue. When these conserved residues were marked in the three dimenetional view of ASK in '''PyMol''', they all seemed clustered within a certain region of the molecule. This region is found in the core of the molecule, directly inside a pocket-like surface feature. This region is assumed to be the 'possible active site' of the protein.  
'''Multiple sequence alighment''' (MSA) revealed some conserved residues throughput the whole sulfatase family. Previous experiemnts on catalytic activity of sulfatases describe a set of residues which are essential for the function of sulfatases. A histidine residue (H)  and two or more '''''sequential''''' arganine residues (R) are known to be essential, and also characteristic of the N-terminal active site of sulfatases. Our MSA resultaed a number of residues conserves in the N-terminus, along with a H and one R residue. When these conserved residues were marked in the three dimenetional view of ASK in '''PyMol''', they all seemed clustered within a certain region of the molecule. This region is found in the core of the molecule, directly inside a pocket-like surface feature. This region is assumed to be the 'possible active site' of the protein.  

Revision as of 06:30, 2 June 2008

Multiple sequence alighment (MSA) revealed some conserved residues throughput the whole sulfatase family. Previous experiemnts on catalytic activity of sulfatases describe a set of residues which are essential for the function of sulfatases. A histidine residue (H) and two or more sequential arganine residues (R) are known to be essential, and also characteristic of the N-terminal active site of sulfatases. Our MSA resultaed a number of residues conserves in the N-terminus, along with a H and one R residue. When these conserved residues were marked in the three dimenetional view of ASK in PyMol, they all seemed clustered within a certain region of the molecule. This region is found in the core of the molecule, directly inside a pocket-like surface feature. This region is assumed to be the 'possible active site' of the protein.


Results of structural comparisons and protein-protein interactions resulted several other proteins, which were used for a second multiple sequence alighment. This alighment also showed a certain degree of conservation of previously described conserved residues.