3bsqA Results
Multiple sequence alignment (MSA) highlighted several residues in N-terminal region of the molecule which are highly conserved ‘‘ (figure 1).
Figure 1: Two sequence alignment of ASK with STS using 'SIM' server, alignment methode' BLOSUM62' with gap penalty of 5 and gap extension penalty of 2.
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 28.1 3.1 342 482 25 MOLECULE: ARYLSULFATASE A; 7: 1e2s-P 28.1 3.0 341 481 26 MOLECULE: ARYLSULFATASE A; 8: 1e3c-P 28.0 3.1 341 481 26 MOLECULE: ARYLSULFATASE A; 9: 1e33-P 28.0 3.1 342 480 25 MOLECULE: ARYLSULFATASE A; 10: 1e1z-P 27.9 3.0 341 481 26 MOLECULE: ARYLSULFATASE A; 11: 1auk 27.8 3.1 340 481 26 MOLECULE: ARYLSULFATASE A; 12: 1p49-A 27.7 2.9 338 548 24 MOLECULE: STERYL-SULFATASE; 13: 1hdh-B 27.4 3.1 365 525 23 MOLECULE: ARYLSULFATASE; 14: 1hdh-A 27.4 3.0 363 525 23 MOLECULE: ARYLSULFATASE; 15: 2rh6-A 24.3 2.6 257 382 14 MOLECULE: PHOSPHODIESTERASE-NUCLEOTIDE PYROPHOSPHATASE; 16: 2rh6-B 24.2 2.6 257 382 14 MOLECULE: PHOSPHODIESTERASE-NUCLEOTIDE PYROPHOSPHATASE;
figure 4: Structural alighment of ASK. 3b5qA and B are two chains of ASK dimer and thired is ASK of Bacterioides fragilis.N-acetylgalactosamine -4- sulfatase, Arylsulfatase A and steryl sulfatase, also known as stroid sulfatase (STS) are most similar protein in structure to ASK. 1hdf is the ASK of Pseudomonal auruginosa.
Subcellular interactions of arylsulfatase K were searched usnig the programme STRING, based on 'neighbourhood', 'cooccurreance' and 'homology' evidence. ‘Putative secreted sulfatase ydeN' only showed neignbourhood relationship, which means that two genes are located in close proximity. In contrast, three of other proteins showed both cooccurrence and homology evidence.
The function of highly related proteins was searched using ProFunc.
Putative Sulfatase YIDI shows sulfuric ester hydrolase activity. Arylsulfatase A possesses phosphoric monester hydrolase activity as well as sulfuric ester hydrolase activity.
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