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== Arylsulfatase K (BT1596) Interactions with other proteins ==
== Arylsulfatase K (BT1596) Interactions with other proteins ==


[[Image:net.png]]
[[Image:net.png|centre|framed|'''figure: 5'''ASK interactions with other proteins. Blue lines indicate cooccurance evidence; red lines, homology and black lines XXX'']]
 
''''figure: 5'''''


   
   

Revision as of 04:44, 7 June 2008

Multiple sequence alignment

Multiple sequence alignment (MSA) highlighted several residues in N-terminal region of the molecule which are highly conserved (figure 1).


Arylsulfatase K structure

Figure 2: Arylsulfatase K as a heterodimer; 3b5q chain A and B


Protein data bank profile characteris arylsulfatase as a hydrolase and a sulfatase. A Sulfatase hydrolyses sulfate esters bonds of substrates, including O-sulfates and N-sulfates as shown below.


ReactionASK.png

figure:3


Structural alignment

  • 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.


  • The function of highly related proteins were found using ProFunc


Arylsulfatase A has both sulfuric ester hydrolase and phosphoric monoester hydrolase activities and localised in lysosomes.
Steryl-sulfatase is a sulfuric ester hydrolase found in endoplasmin reticulums.


Arylsulfatase K (BT1596) Interactions with other proteins

figure: 5ASK interactions with other proteins. Blue lines indicate cooccurance evidence; red lines, homology and black lines XXX


Input Protein

  • BT1596 Putative sulfatase yidJ (481 aa) of Bacteroides thetaiotaomicron.

Predicted Functional Partners

  • BT3796: Putative secreted sulfatase ydeN (518 aa).
  • BT1595 Transcription termination factor rho (722 aa).
  • BT1597 Two-component system sensor histidine kinase (539 aa).
  • BT3057 N-acetylgalactosamine-6-sulfatase (508 aa).
  • BT1598 Putative two-component system sensor histidine (655 aa).
  • BT3101 N-sulphoglucosamine sulphohydrolase (455 aa).
  • BT3489 Arylsulfatase B {UniProtKB/TrEMBL-Q8A219} (458 aa).


ProFunc results for ASK interacting proteins.

  • 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
  • N-acetylgalactosamine-4- sulfatase (Arylsulfatase B) hydrolyse the sulfate ester group from N-acetylgalactosamine 4-sulfate of dermatine sulfate. Deficiency of ASB cause a rare mucopolysaccharidosis (MPS IV; Maroteaux-Lamy syndrome)

All these enzymes has generaly the same function, but acts on different substrate.


Two sequence alignment of ASK and STS

STS was chossen to be the most similar enzyme to ASK due to the shired subcellylar localization. Two sequence alignmnt between ASK and STS is shown is figure: 6.


Figure: 6 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