COASY results: Difference between revisions

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|Cell 1 || Cell 2 || Cell 3
|Cell 1 || Cell 2 || Cell 3
|-
|-
|Cell A  
|Pattern-ID: GLYCOSAMINOGLYCAN PS00002 PDOC00002
|Cell B
|Pattern-DE: Glycosaminoglycan attachment site
|Cell C
|Pattern: SG.G
|Position: 84 SGSG
|Pattern-ID: PKC_PHOSPHO_SITE PS00005 PDOC00005
|Pattern-DE: Protein kinase C phosphorylation site
|Pattern: Pattern: [ST].[RK]
|Position: 3 SDK
|Position: 52 SFR
|Position: 86 SGK
|Pattern-ID: CK2_PHOSPHO_SITE PS00006 PDOC00006
|Pattern-DE: Casein kinase II phosphorylation site
|Pattern: [ST].{2}[DE]
|Position: 39 SHNE
|Position: 251 TLWE
|Position: 260 SQVE
|Pattern-ID: MYRISTYL PS00008 PDOC00008
|Pattern-DE: N-myristoylation site
|Pattern: G[^EDRKHPFYW].{2}[STAGCN][^P]
|Position: 82 GISGSG
|Position: 222 GLSEAA
|Pattern-ID: ATP_GTP_A PS00017 PDOC00017
|Pattern-DE: ATP/GTP-binding site motif A (P-loop)
|Pattern: [AG].{4}GK[ST]
|Position: 82 GISGSGKS
|Pattern-ID: UPF0038 PS01294 PDOC00996
|Pattern-DE: Uncharacterized protein family UPF0038 signature
|Pattern: G.[LI].R.{2}L.{4}F.{8}[LIV].{5}P.[LIV]
|Position: 136 GTINRKVLGSRVFGNKKQMKILTDIVWPVI
|}
|}



Revision as of 13:31, 9 June 2007

Structure of Coenzyme A Synthase

Conezyme A Synthase is structurally composed of seven strands, eleven helices and thirteen beta turns (EMBL EBI, 2005) (see Figure 1). Analysis of structurally related proteins (Holm & Sander, 1993) showed a trend for transferase (RCSB, 2007) class proteins with Rossmann class folds (Rossmann, 1973). The Rossmann topologies of fold’s are an alpha-beta class fold that forms a three or more layer beta strand sandwich alternating with alpha helices (beta-alpha-beta-alpha-beta). PFAM classification placed these into either the Cytidylyltransferase or Dephospho-CoA kinase familes, matching the two domains of Coenzyme A Synthase. Those classified under the Dephospho-CoA kinase type were commonly of the P-loop containing nucleotide triphosphate hydrolases (Sanger Institute, 2005) homology whilst those classified as Cytidylyltransferase were of the Tyrosol-Transfer RNA Synthetase (Sanger Institute, 2005). As the majority of the structurally related proteins identified contained the DPCK domain solely, and the motif for a P-loop (Table 1) was identified in the Conzyme A Synthase sequence (Bairoch, Bucher, & Hofmann, 1997) it is suggested that Coenzyme A Synthase is also of the P-loop containing nucleotide triphosphate hydrolases homology of folds.


Table 1

PROSITE Motif search (Bairoch, Bucher, & Hofmann, 1997) results on Coenzyme A Synthase: Mus. musculus.
Cell 1 Cell 2 Cell 3
Pattern-ID: GLYCOSAMINOGLYCAN PS00002 PDOC00002 Pattern-DE: Glycosaminoglycan attachment site Pattern: SG.G Position: 84 SGSG Pattern-ID: PKC_PHOSPHO_SITE PS00005 PDOC00005 Pattern-DE: Protein kinase C phosphorylation site Pattern: Pattern: [ST].[RK] Position: 3 SDK Position: 52 SFR Position: 86 SGK Pattern-ID: CK2_PHOSPHO_SITE PS00006 PDOC00006 Pattern-DE: Casein kinase II phosphorylation site Pattern: [ST].{2}[DE] Position: 39 SHNE Position: 251 TLWE Position: 260 SQVE Pattern-ID: MYRISTYL PS00008 PDOC00008 Pattern-DE: N-myristoylation site Pattern: G[^EDRKHPFYW].{2}[STAGCN][^P] Position: 82 GISGSG Position: 222 GLSEAA Pattern-ID: ATP_GTP_A PS00017 PDOC00017 Pattern-DE: ATP/GTP-binding site motif A (P-loop) Pattern: [AG].{4}GK[ST] Position: 82 GISGSGKS Pattern-ID: UPF0038 PS01294 PDOC00996 Pattern-DE: Uncharacterized protein family UPF0038 signature Pattern: G.[LI].R.{2}L.{4}F.{8}[LIV].{5}P.[LIV] Position: 136 GTINRKVLGSRVFGNKKQMKILTDIVWPVI

Figure 1

The secondary structure of Mus musculus with indicated ligand interaction sites (EMBL EBI, 2005).
COASYSecondary structure with bind sites.gif


Figure 2

Structural alignment of structurally related proteins to Mus. musculus Coenzyme A Synthase
COASYStructureconservationstructurealignment.JPG


Localisation Expression of Coenzyme A Synthase

Sequence Conservation of Coenzyme A Synthase

Structural Elements and Functional Binding Sites of Coenzyme A Synthase


Abstract | Introduction | Results | Discussion | Conclusion | Method | References

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