3bsqA Results: Difference between revisions
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'''MSA''' highlited sevlral residues which are | '''MSA''' highlited sevlral residues in N-terminal region of the molecule which are highly conserved ''(figure 1)''. | ||
The three dimentional structure was viewed using '''PyMol''' ''(figure 2)'' and these conserved residues were marked on the crystal structure. However they were not related to binding sited of Cl and Zn, but buried in the core of the protein within a pocket-like region ''(figure 3)''. | |||
The three dimentional structure of the enzyme was viewed using '''PyMol''' ''(figure 2)'' and these conserved residues were marked on the crystal structure. However they were not related to binding sited of Cl and Zn, but buried in the core of the protein within a pocket-like region ''(figure 3)''. | |||
All attempts to see the electrostatic nature of this pocket were unsuccessful, due to some technical probloems with '''PyMol'''. | All attempts to see the electrostatic nature of this pocket were unsuccessful, due to some technical probloems with '''PyMol'''. | ||
Three dimentional structure of arylsulfatase was aligned with other available structures using DALI server [http://ekhidna.biocenter.helsinki.fi/dali_server/results/20080513-017-30c6150342a20dabd7c2488208032bb4 (structural alignment)]. Results are shown in 'figure 4'. | Three dimentional structure of arylsulfatase was aligned with other available structures using '''DALI''' server [http://ekhidna.biocenter.helsinki.fi/dali_server/results/20080513-017-30c6150342a20dabd7c2488208032bb4 (structural alignment)]. Results are shown in 'figure 4'. | ||
Revision as of 09:09, 2 June 2008
MSA highlited sevlral residues in N-terminal region of the molecule which are highly conserved (figure 1).
The three dimentional structure of the enzyme was viewed using PyMol (figure 2) and these conserved residues were marked on the crystal structure. However they were not related to binding sited of Cl and Zn, but buried in the core of the protein within a pocket-like region (figure 3). All attempts to see the electrostatic nature of this pocket were unsuccessful, due to some technical probloems with PyMol.
Three dimentional structure of arylsulfatase was aligned with other available structures using DALI server (structural alignment). Results are shown in 'figure 4'.
No: Chain Z rmsd lali nres %id Description 1: 3b5q-A 73.6 0.0 464 464 100 MOLECULE: PUTATIVE SULFATASE YIDJ; 2: 3b5q-B 70.2 0.3 464 467 100 MOLECULE: PUTATIVE SULFATASE YIDJ; 3: 2qzu-A 35.1 2.5 375 465 25 MOLECULE: PUTATIVE SULFATASE YIDJ; 4: 1fsu 28.7 2.8 344 474 22 MOLECULE: N-ACETYLGALACTOSAMINE-4-SULFATASE; 5: 1n2l-A 28.4 3.0 343 483 25 MOLECULE: ARYLSULFATASE A; 6: 1n2k-A 28.3 3.2 344 482 25 MOLECULE: ARYLSULFATASE A; 7: 1e3c-P 28.2 3.2 344 481 26 MOLECULE: ARYLSULFATASE A; 8: 1e33-P 28.2 3.1 344 480 25 MOLECULE: ARYLSULFATASE A; 9: 1e2s-P 28.2 3.1 343 481 25 MOLECULE: ARYLSULFATASE A; 10: 1e1z-P 28.1 3.2 344 481 26 MOLECULE: ARYLSULFATASE A; 11: 1auk 27.9 3.1 343 481 25 MOLECULE: ARYLSULFATASE A;
Figure 4: Structurally related proteins. (No 1 and 2 are two chains of arylsulfatase K).
The function of highly related proteins were found using ProFunc.
Putative Sulfatase YIDI hydrolyses sulfuric ester bonds of its substrate hence significant in metabolism. Arylsulfatase A has both sulfuric ester hydrolase and phosphoric monoester hydrolase activities.
Protein interactions of arylsulfatase K with other proteis were vieved usig the server STRING, which revealed four major hits, depending on 'neighbourhood', 'cooccurreance' and 'homology' evidence. 'Putative secreted sulfatase ydeN' only showed neignbourhood relationship, which means that their genes are located in close proximity. But three of other proteins showed both cooccurrence and homology evidence, therefore their functions were analysed with ProFunc.
N-acetylgalactosamine-6-sulfatase cleaves the 6-sulfate groups of N-acetyl-D-galactosamine 6-sulfate units in chondroitin sulfate and D-galactose 6-sulfate units in keratan sulfate. N-sulphoglucosamine sulphohydrolase is also known as heparine sulfamidase, which catalyses the hydrolysis of Sulfur-Nitrogen bonds. N-sulphoglucosamine sulphohydrolase is responsible for the degradation of glucosaminlglycan and glycan structure of extra cellular matrix.
- N-sulfo-D-glucosamine + H(2)O <=> D-glucosamine + sulfate