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The predicted function based on the evolution and structure
The predicted function based on the evolution and structure


<font size = "4">'''Hydrolase'''</font>


<font size = "4">'''Hyrolyase'''</font>


[[Image:Document18_01.png]]
[[Image:Document18_01.png]]
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<font size = "4">'''Pfam'''</font>


== Function of sulfatases ==


{|cellspacing="0" cellpadding = "10" style="border-style:solid; border-color:black; border-width:1px;"
Sulfatases are enzymes,which hydrolyse sulfate ester bonds of substrates.
Most of the family members has shown to contain a highly conserved cystine residue and a bivalent metal binding site.
Hydrolase: domain 1 of 1, from 18 to 224: score 96.2, E = 1e-25
                  *->ikavvFDkDGTLtdgkeppiaeaiveaaaelgl.........lplee
                      ++av+FD+D+TL+d+ + + ++ + e+ ++l  + + +++ ++  +
      query    18    VRAVFFDLDNTLIDT-AGASRRGMLEVIKLLQSkyhykeeaeIICDK 63 


                  vekllgrgl.g.erilleggltaell...................d.evl
                  v  l +++ ++    ++  t ++ +  +++++ ++++  ++    ++
      query    64 VQVKLSKECfHpYSTCITDVRTSHWEeaiqetkggadnrklaeecYfLWK 113


                  glial.dklypgarealkaLkrrGikvailTggdr.naeallealgla.l
                    ++ ++  l +++++ l +L++  +++ +lT+gdr++++++ ea+++ ++
      query  114 STRLQhMILADDVKAMLTELRKE-VRLLLLTNGDRqTQREKIEACACQsY 162


                  fdviidsdevggvgpivvgKPkpeifllalerlgvkpeevgpevlmVGDg
                  fd+i++++e +        KP+p if + ++ lgv+p ++    +mVGD+
      query  163 FDAIVIGGEQK------EEKPAPSIFYHCCDLLGVQPGDC----VMVGDT 202


                  vnDapalaa.AGv.gvamgngg<-*
                  + +++ +  +AG+++++++n + 
      query  203 LETDIQGGLnAGLkATVWINKS    224 
|}
The alignments of the top-scoring domains of 2gfh (query) protein using Pfam 21.0 (Janelia Farm). ([http://pfam.janelia.org/ http://pfam.janelia.org])
* Shows the highest scored match - Hydrolase
* Score  = 96.2
* E value = 1e-25
<font size = "4">'''Gene Ontology'''</font>
[[Image:Document17_01.png]]
List of all matched protein name terms for 2gfh. The score in red is a measure of how strongly the term is predicted from the hits obtained by
the different methods. The scores in blue show each method<nowiki>’</nowiki>s contribution to the total score (with the number of relevant
sequences/structures shown in brackets in grey).(http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/)
* Higest score in GO - Hydrolase
* Followed by - Phosphatase
*Polymer:            Haloacid dehalogenase-like hydrolase domain containing 4
*Molecular Function: None
*Biological Process: None
*Cellular Component: None
<font size = "4">'''Surface Properties'''</font>
[[Image:Document7_07.png]]
'''Figure 13. (A) '''Molecular structure of 2gfh with the ligand PO<sub>4.</sub>''' (B) '''Molecular and chemical structure of PO<sub>4.</sub>'''  (C) '''Ligand interaction involving PO<sub>4.</sub> (Picture adapted from Profunc)
* Identify the likely biochemical function from the 3D structure
* Possible binding sites and potential ligands - PO<sub>4</sub>
* PO<sub>4</sub> most likely be an active site and fuction
<font size = "4">'''Phostphatase'''</font>
[[Image:Document9_01.png]]
MSA of the 2gfh with 35 others proteins. Only the 60<sup>th</sup> – 70<sup>th</sup> and the 210<sup>th</sup> -300<sup>th</sup> amino acid
sequence were shown to illustrate the conserved and invariant regions. The 3 boxed-up sequences were either conserved or invariant regions.
* 1st - aspartic acid (D)
* 2nd - threonine (T), asparagine (N) and glycine (G)
* 3rd - lysine (K) and aspartates (D)
* MSA corelate with with study done by Maliekal et al
**N-acetylneuraminic acid phosphatase orthologs shared 3 motifs found in phosphatases
*HAD (Haloacid dehalogenase-like) family
** Phosphatase activity:  CO–P bond hydrolysis
** Dehalogenase activity:  C–halogen bond hydrolysis
** Phosphonatase:          C–P bond hydrolysis
** Phosphoglucomutase:    CO–P bond hydrolysis and intramolecular phosphoryl transfer
<font size = "4">'''Role in Human'''</font>
* OMIM
** Haloacid dehalogenase-like hydrolase domain
** Gene map locus 20p11
[[Image:Document2_01.png]]
Dephosphorylation of Neu5Ac-9-P is a reversible reaction with an end product of Neu5Ac (sialic acid) and a free phosphate.
* Main form of sialic acid in vertebrates
** Important roles in protein-protein and cell-cell recognition
** Dependent on the presence of Mg<sup>2+</sup>
** Inhibited by vanadate and Ca<sup>2+</sup>
<font size = "4">'''Role in Bacteria - ''E.coli'''''</font>
* Hydrolyze a wide range of phosphorylated metabolites
** Carbohydrates
** Nucleotides,
** Organic acids
* Kuznetsova ''et al'' - glycolysis and pentose phosphate pathway
** Fructose-1-phosphate
** Glucose-6-phosphate
** Mannose-6-phosphate
** 2-deoxyglucose-6-phosphate
** Fructose-6- phosphate
** Ribose-5-phosphate
** Erythrose- 4-phosphate
[[Image:Document20_01.png]]
[[Image:Document20_02.png]]
Schematic diagrams of glycolysis and pentose phosphate metabolic pathways. The green arrows show the substrates that are hydrolyzed by HADs (http://www.steve.gb.com/science/core_metabolism.html)
[[N-acetylneuraminic acid phosphatase| Previous page]]
[[Pfam| Next page]]


== Functional site==
MSA data revealed some conserved residues on the sequence. They were mapped on the three dimantional structure.


[[Image:Zn_Cl_surface]]


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Latest revision as of 09:44, 20 May 2008

The predicted function based on the evolution and structure

Hydrolase


Document18 01.png

Hydrolyase catalyze the hydrosis of the chemical bond between A and B, resulting of 2 simple molecules


  • Hydrolase
    • Catalyze hydrolysis reaction
    • Addition of the hydrogen and hydroxyl ions of water
    • Splitting into 2 or more simpler molecules
    • EC class 3


Function of sulfatases

Sulfatases are enzymes,which hydrolyse sulfate ester bonds of substrates. Most of the family members has shown to contain a highly conserved cystine residue and a bivalent metal binding site.



Functional site

MSA data revealed some conserved residues on the sequence. They were mapped on the three dimantional structure.

File:Zn Cl surface


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