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BPP22:CAPSD
Contents
| Species (Taxon ID) | Salmonella phage P22 (Bacteriophage P22). (10754) | |
| Gene Name(s) | 5 | |
| Protein Name(s) | Major capsid protein (ECO:0000305)
Gene product 5 (ECO:0000305) gp5 Major head protein (ECO:0000305) | |
| External Links | ||
| UniProt | P26747 | |
| EMBL | M59749 AF217253 BK000583 AF527608 AB362338 AB426868 | |
| PIR | E40474 | |
| RefSeq | NP_059630.1 | |
| PDB | 2M5S 2XYY 2XYZ 3IYH 3IYI | |
| PDBsum | 2M5S 2XYY 2XYZ 3IYH 3IYI | |
| SMR | P26747 | |
| DIP | DIP-29111N | |
| GeneID | 1262831 | |
| KEGG | vg:1262831 | |
| OrthoDB | VOG0900009D | |
| EvolutionaryTrace | A8CGC7 P26747 | |
| Proteomes | UP000001315 UP000001795 UP000001796 UP000002165 UP000007960 | |
| GO | GO:0039620 | |
| InterPro | IPR024659 | |
| Pfam | PF11651 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0046797 |
viral procapsid maturation |
ECO:0000315 |
P |
Mutant phenotypes D244A and D246A were used to show the role of the D-loop in procapsid maturation. In figure 2A, the wild type shows 2 peaks corresponding to procapsid protein around fraction 16 and mature phages that incorporated the coat protein at fraction 23. D244A mutant showed improperly formed procapsids in figure 2B which could correspond to the protein peak at fraction 16 in figure 2A. D244A showed very little coat protein at fraction 23 indicating phages were not produced. The D246A mutants showed no significant amount of procapsid protein at fraction 16. In figure 2B the D246A mutant showed particles that were incomplete instead of procapsid proteins that were present in wild types. This mutant also showed no peak of mature coat protein at fraction 23 indicating the phages were not able to form. |
complete | |||||
| GO:0046729 |
viral procapsid |
ECO:0000314 |
C |
Figure 7. By testing disulfold crosslink form or not among purified proteins N245/C405S and L243C/C405 under room temperature and high temperature, they conclude that tips of the D-loop locates in close proximity at the 2-fold axis between coat sub-units both in capsid and precapsid. And the tips would remain in proximity after capsid expansion. |
complete | |||||
| GO:0039620 |
T=7 icosahedral viral capsid |
ECO:0000314 |
C |
Gp5 of Salmonella phage P22 was shown to fold into a classical HK97 capsid fold (PMID:11000116[3]). Figure 1b shows a density map of the P22 capsid cryo-EM model. From the cryo-EM image, one asymmetrical unit, outlined in red in Figure 1b, was modeled and presented in Figure 1c with seven different colors representing each of the seven proteins folding into a T=7 icosahedral structure. This cryo-EM derived model of the protein matched closely to the molecular model of the gp5 430 amino acid sequence shown in Figure 2b. This 430 amino acid sequence number corresponds to the BLAST sequence in Uniprot for gp5, confirming that the model derived from the cryo-EM imaging was indeed gp5. |
complete | |||||
| GO:0019070 |
viral genome maturation |
ECO:0000315 |
P |
Figure 2. In the first graph, which shows the levels of labeled DNA from Intermediate I (the DNA replication complex), the 5- mutant's Intermediate I radioactivity level is 23%. Comparatively, the wild type radioactivity is 4% in the Intermediate I at the same time mark. In the second graph, which shows the radioactivity in the mature DNA region, the radioactivity from the 5- mutant's mature DNA region is 33%. Comparatively, the wild type phage's mature DNA region radioactivity level is 85%. |
complete | |||||
|
part_of |
GO:0039620 |
T=7 icosahedral viral capsid |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0046729 |
viral procapsid |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0042803 |
protein homodimerization activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0019028 |
viral capsid |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0046797 |
viral procapsid maturation |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0019012 |
virion |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0019028 |
viral capsid |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0039620 |
T=7 icosahedral viral capsid |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 D'Lima, NG & Teschke, CM (2015) A Molecular Staple: D-Loops in the I Domain of Bacteriophage P22 Coat Protein Make Important Intercapsomer Contacts Required for Procapsid Assembly. J. Virol. 89 10569-79 PubMed GONUTS page
- ↑ Hryc, CF et al. (2017) Accurate model annotation of a near-atomic resolution cryo-EM map. Proc. Natl. Acad. Sci. U.S.A. 114 3103-3108 PubMed GONUTS page
- ↑ Wikoff, WR et al. (2000) Topologically linked protein rings in the bacteriophage HK97 capsid. Science 289 2129-33 PubMed GONUTS page
- ↑ Botstein, D et al. (1973) Mechanism of head assembly and DNA encapsulation in Salmonella phage p22. I. Genes, proteins, structures and DNA maturation. J. Mol. Biol. 80 669-95 PubMed GONUTS page
- ↑ Chen, DH et al. (2011) Structural basis for scaffolding-mediated assembly and maturation of a dsDNA virus. Proc. Natl. Acad. Sci. U.S.A. 108 1355-60 PubMed GONUTS page
- ↑ 6.0 6.1 6.2 6.3 Kang, S & Prevelige, PE Jr (2005) Domain study of bacteriophage p22 coat protein and characterization of the capsid lattice transformation by hydrogen/deuterium exchange. J. Mol. Biol. 347 935-48 PubMed GONUTS page
- ↑ Parent, KN et al. (2010) P22 coat protein structures reveal a novel mechanism for capsid maturation: stability without auxiliary proteins or chemical crosslinks. Structure 18 390-401 PubMed GONUTS page
- ↑ Tang, L et al. (2006) Highly discriminatory binding of capsid-cementing proteins in bacteriophage L. Structure 14 837-45 PubMed GONUTS page
