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User:Farooquenb

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Phage Hunters Spring 2017

My Annotations

StatusPageDate/TimeGO Term (Aspect)ReferenceEvidenceNotesLinks
flaggedBPE15:Q858G82017-04-12 13:47:16 CDTGO:0019028 viral capsid (C)PMID:23840063ECO:0000250 sequence similarity evidence used in manual assertion

Figure S6 in the supporting information document shows the structural homologs of gp7. Gp7 is a protein subunit of the capsid of epsilon15. The overall structure of gp7 is similar to the canonical bacteriophage coat proteins in tailed dsDNA bacteriophage. When the gp7 model is compared to the gp5 of HK97, the two structures are remarkably very similar. The two structures are nearly identical for about the first 145 amino acids. However, a domain swap in gp7 creates a 55% structural similarity according to CLICK. The two structures have a topology score of 1.0 according to CLICK. Therefore, the high structural similarity between HK97 gp5 and e15 gp7, provides further validation of the gp7 model. The evolutionary lineage of the e15 phage shows a highly conserved structural folding as supported by gp5 of HK97.

challenge
flaggedBPE15:Q858G82017-04-12 13:53:58 CDTGO:0019028 viral capsid (C)PMID:23840063ECO:0000250 sequence similarity evidence used in manual assertion

X-ray crystallographic modeling tools were used to refine gp10 models. The gp10 refined model depicts an eight-stranded jellyroll fold. Using DALI, structural similarity was determined among various viruses with the same jellyroll fold. Figure S8 shows the structural homologs of the gp10 models. Gp10 is a protein subunit of the capsid of bacteriophage, epsilon15. Part A of figure S8 shows gp10's interaction with the exposed surface and the capsid surface. According to DALI, the top score of structural similarity to the gp10 of epsilon15 was given to the projecting jellyroll domain of the virus VP2 (PDB ID: 2DF7, Z-score = 6.3). Despite a difference in its length and sequence, gp10 and 2DF7 domain structure share a similar folding pattern. The topology of these two structures are identical. The high structural match between these two structures further validates the gp10 model.

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