Sand box 326: Difference between revisions

From Proteopedia
Jump to navigationJump to search
No edit summary
No edit summary
Line 29: Line 29:
Similar conserved sequences could be found between 4Q7Q and lipases. The GDSI, GxND, and DGxH sequences can be seen from lipases like 7BXD.? The same secondary structure segments can also be located in the lipases analyzed.
Similar conserved sequences could be found between 4Q7Q and lipases. The GDSI, GxND, and DGxH sequences can be seen from lipases like 7BXD.? The same secondary structure segments can also be located in the lipases analyzed.


== Structural Analysis ==  
== Structural Analysis (DONE) ==  


Right-hand SPRITE analysis revealed 4Q7Q exhibited residues like those seen from enzymes operating with acetyl-like substrates. Specifically, residues Ser. 30, Gly. 69, Asn. 97, Asp. 251, and His. 254 on the A and B chains of 4Q7Q line up with similarly positioned residues on esterases like Platelet-Activating Factor Acetylhyd (PAFA), which exhibited an RMSD of 0.25 angstroms when compared to 4Q7Q.
Using Right-hand SPRITE analysis, it showed that 3BCW had similar residues to small amino acid chains. Specific residues are Ala. 76, Ile. 79, Gly. 61, Val. 293, the first two being on the A chain side and the second being on the B chain side of the 3CBW. Comparing 3CBW to 1BHG, which is human beta-glucuronidase, the RMSD value was a difference of 0.46 angstroms.  


Other proteins with similar motifs of note are Thioesterase I and Rhamnogalacturonan Acetylesterase, with RMSD values of 0.46 and 0.61, respectively. These alignments focus on the same active site as PAFA did, suggesting the acetyl-like substrates 4Q7Q focuses on are similar to esters.
With the use of DALI, it was determined that 3CBW is most similar to Beta-1,4-Mannanase and Mannan Endo-1,4-Beta-Mannosidase. Both of these enzymes hydrolyzes different linkages.  


PFAM graphics from DALI revealed significant structural equivalence between 4Q7Q, a lipase-like protein, Rhamnogalacturonan Acetylesterase, and Sialate O-acetylesterase.


== Substrates ==
== Substrates ==