2bpa

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(Difference between revisions)

Revision as of 13:15, 24 November 2021

ATOMIC STRUCTURE OF SINGLE-STRANDED DNA BACTERIOPHAGE PHIX174 AND ITS FUNCTIONAL IMPLICATIONS

Structural highlights

2bpa is a 4 chain structure with sequence from Bpphx. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[J_BPPHX] Mediates ssDNA packaging into virion, it locates to the internal surface of the capsid, thereby displacing the internal scaffolding protein B during virion formation. Additionally, protein J plays a role in viral attachment to the host cell. [G_BPPHX] Attaches the circulating virion to the bacterial lipopolysaccharides which serve as receptor for the virus. Determines the phage host-range. Probably triggers with protein H the injection of the phage DNA into the host cytoplasm upon conformational changes induced by the interaction with host lipopolysaccharides.^[1] ^[2] [F_BPPHX] Assembles to form an icosahedral capsid with a T=1 symmetry, about 30 nm in diameter, and consisting of 60 capsid proteins F.^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The mechanism of DNA ejection, viral assembly and evolution are related to the structure of bacteriophage phi X174. The F protein forms a T = 1 capsid whose major folding motif is the eight-stranded antiparallel beta barrel found in many other icosahedral viruses. Groups of 5 G proteins form 12 dominating spikes that enclose a hydrophilic channel containing some diffuse electron density. Each G protein is a tight beta barrel with its strands running radially outwards and with a topology similar to that of the F protein. The 12 'pilot' H proteins per virion may be partially located in the putative ion channel. The small, basic J protein is associated with the DNA and is situated in an interior cleft of the F protein. Tentatively, there are three regions of partially ordered DNA structure,

Atomic structure of single-stranded DNA bacteriophage phi X174 and its functional implications.,McKenna R, Xia D, Willingmann P, Ilag LL, Krishnaswamy S, Rossmann MG, Olson NH, Baker TS, Incardona NL Nature. 1992 Jan 9;355(6356):137-43. PMID:1370343^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Inagaki M, Tanaka A, Suzuki R, Wakashima H, Kawaura T, Karita S, Nishikawa S, Kashimura N. Characterization of the binding of spike H protein of bacteriophage phiX174 with receptor lipopolysaccharides. J Biochem. 2000 Apr;127(4):577-83. PMID:10739948
↑ Inagaki M, Kawaura T, Wakashima H, Kato M, Nishikawa S, Kashimura N. Different contributions of the outer and inner R-core residues of lipopolysaccharide to the recognition by spike H and G proteins of bacteriophage phiX174. FEMS Microbiol Lett. 2003 Sep 26;226(2):221-7. PMID:14553915
↑ Hafenstein S, Fane BA. phi X174 genome-capsid interactions influence the biophysical properties of the virion: evidence for a scaffolding-like function for the genome during the final stages of morphogenesis. J Virol. 2002 Jun;76(11):5350-6. PMID:11991963
↑ McKenna R, Xia D, Willingmann P, Ilag LL, Krishnaswamy S, Rossmann MG, Olson NH, Baker TS, Incardona NL. Atomic structure of single-stranded DNA bacteriophage phi X174 and its functional implications. Nature. 1992 Jan 9;355(6356):137-43. PMID:1370343 doi:http://dx.doi.org/10.1038/355137a0

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bpa"

@@ Line 3: / Line 3: @@
 <StructureSection load='2bpa' size='340' side='right'caption='[[2bpa]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2bpa]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpphx Bpphx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BPA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BPA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2bpa]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpphx Bpphx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BPA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BPA FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bpa OCA], [http://pdbe.org/2bpa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bpa RCSB], [http://www.ebi.ac.uk/pdbsum/2bpa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bpa ProSAT]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bpa OCA], [https://pdbe.org/2bpa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bpa RCSB], [https://www.ebi.ac.uk/pdbsum/2bpa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bpa ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/J_BPPHX J_BPPHX]] Mediates ssDNA packaging into virion, it locates to the internal surface of the capsid, thereby displacing the internal scaffolding protein B during virion formation. Additionally, protein J plays a role in viral attachment to the host cell. [[http://www.uniprot.org/uniprot/G_BPPHX G_BPPHX]] Attaches the circulating virion to the bacterial lipopolysaccharides which serve as receptor for the virus. Determines the phage host-range. Probably triggers with protein H the injection of the phage DNA into the host cytoplasm upon conformational changes induced by the interaction with host lipopolysaccharides.<ref>PMID:10739948</ref> <ref>PMID:14553915</ref>  [[http://www.uniprot.org/uniprot/F_BPPHX F_BPPHX]] Assembles to form an icosahedral capsid with a T=1 symmetry, about 30 nm in diameter, and consisting of 60 capsid proteins F.<ref>PMID:11991963</ref>
+[[https://www.uniprot.org/uniprot/J_BPPHX J_BPPHX]] Mediates ssDNA packaging into virion, it locates to the internal surface of the capsid, thereby displacing the internal scaffolding protein B during virion formation. Additionally, protein J plays a role in viral attachment to the host cell. [[https://www.uniprot.org/uniprot/G_BPPHX G_BPPHX]] Attaches the circulating virion to the bacterial lipopolysaccharides which serve as receptor for the virus. Determines the phage host-range. Probably triggers with protein H the injection of the phage DNA into the host cytoplasm upon conformational changes induced by the interaction with host lipopolysaccharides.<ref>PMID:10739948</ref> <ref>PMID:14553915</ref>  [[https://www.uniprot.org/uniprot/F_BPPHX F_BPPHX]] Assembles to form an icosahedral capsid with a T=1 symmetry, about 30 nm in diameter, and consisting of 60 capsid proteins F.<ref>PMID:11991963</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2bpa

From Proteopedia

Revision as of 13:15, 24 November 2021

ATOMIC STRUCTURE OF SINGLE-STRANDED DNA BACTERIOPHAGE PHIX174 AND ITS FUNCTIONAL IMPLICATIONS

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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