1al0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:31, 7 February 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='1al0' size='340' side='right'caption='[[1al0]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
<StructureSection load='1al0' size='340' side='right'caption='[[1al0]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[1al0]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacteria_phage_phix174 Enterobacteria phage phix174]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AL0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AL0 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[1al0]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_phiX174 Escherichia virus phiX174]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AL0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AL0 FirstGlance]. <br>
-
</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=1al0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1al0 OCA], [https://pdbe.org/1al0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1al0 RCSB], [https://www.ebi.ac.uk/pdbsum/1al0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1al0 ProSAT]</span></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#8491;</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=1al0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1al0 OCA], [https://pdbe.org/1al0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1al0 RCSB], [https://www.ebi.ac.uk/pdbsum/1al0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1al0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/B_BPPHX B_BPPHX]] Participates in the assembly of the viral procapsid in the cytoplasm. Forms first a 12S pre-assembly complex with protein H, and F and G pentamers, then twelve 12S complexes are joined by the D protein to form the procapsid. Internal scaffold protein B is released from the procapsid upon genome packaging, possibly through affinity displacement by the protein J, or by proteolysis. [[https://www.uniprot.org/uniprot/D_BPPHX D_BPPHX]] Assembles the procapsid by joining twelve 12S pre-assembly complex into a T=1 icosahedral particle, called 108S procapsid. Ten proteins D bind each 12S complex, which are formed by three pentamers of F, G, B protein and a H protein. The scaffolding protein is released from the provirion after genome packaging to form the mature virion.<ref>PMID:159449</ref> <ref>PMID:15890913</ref> [[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>
+
[https://www.uniprot.org/uniprot/SCAFD_BPPHS SCAFD_BPPHS] Assembles the procapsid by joining twelve 12S pre-assembly complex into a T=1 icosahedral particle, called 108S procapsid. Ten proteins D bind each 12S complex, which are formed by three pentamers of F, G, B protein and a H protein. The scaffolding protein is released from the provirion after genome packaging to form the mature virion.<ref>PMID:15890913</ref> <ref>PMID:159449</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 18: Line 19:
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1al0 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1al0 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
-
<div style="background-color:#fffaf0;">
 
-
== Publication Abstract from PubMed ==
 
-
The assembly of a macromolecular structure proceeds along an ordered morphogenetic pathway, and is accomplished by the switching of proteins between discrete conformations as they are added to the nascent assembly. Scaffolding proteins often play a catalytic role in the assembly process, rather like molecular chaperones. Although macromolecular assembly processes are fundamental to all biological systems, they have been characterized most thoroughly in viral systems, such as the icosahedral Escherichia coli bacteriophage phiX174. The phiX174 virion contains the proteins F, G, H and J. During assembly, two scaffoldingproteins B and D are required for the formation of a 108S, 360-A-diameter procapsid from pentameric precursors containing the F, G and H proteins. The procapsid contains 240 copies of protein D, forming an external scaffold, and 60 copies each of the internal scaffolding protein B, the capsid protein F, and the spike protein G. Maturation involves packaging of DNA and J proteins and loss of protein B, producing a 132S intermediate. Subsequent removal of the external scaffold yields the mature virion. Both the F and G proteins have the eight-stranded antiparallel beta-sandwich motif common to many plant and animal viruses. Here we describe the structure of a procapsid-like particle at 3.5-A resolution, showing how the scaffolding proteins coordinate assembly of the virus by interactions with the F and G proteins, and showing that the F protein undergoes conformational changes during capsid maturation.
 
- 
-
Structure of a viral procapsid with molecular scaffolding.,Dokland T, McKenna R, Ilag LL, Bowman BR, Incardona NL, Fane BA, Rossmann MG Nature. 1997 Sep 18;389(6648):308-13. PMID:9305849<ref>PMID:9305849</ref>
 
- 
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
-
</div>
 
-
<div class="pdbe-citations 1al0" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Enterobacteria phage phix174]]
+
[[Category: Escherichia virus phiX174]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Dokland, T]]
+
[[Category: Dokland T]]
-
[[Category: Rossmann, M G]]
+
[[Category: Rossmann MG]]
-
[[Category: Bacteriophage]]
+
-
[[Category: Chaperone]]
+
-
[[Category: Icosahedral virus]]
+
-
[[Category: Procapsid]]
+
-
[[Category: Scaffolding protein]]
+
-
[[Category: Virus]]
+

Current revision

PROCAPSID OF BACTERIOPHAGE PHIX174

PDB ID 1al0

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools