1tx9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1tx9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tx9, resolution 3.31&Aring;" /> '''gpd prior to capsid ...)
Current revision (06:35, 23 August 2023) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1tx9.gif|left|200px]]<br /><applet load="1tx9" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1tx9, resolution 3.31&Aring;" />
 
-
'''gpd prior to capsid assembly'''<br />
 
-
==Overview==
+
==gpd prior to capsid assembly==
-
The three-dimensional structure of bacteriophage phiX174 external, scaffolding protein D, prior to its interaction with other structural, proteins, has been determined to 3.3 angstroms by X-ray crystallography., The crystals belong to space group P4(1)2(1)2 with a dimer in the, asymmetric unit that closely resembles asymmetric dimers observed in the, phiX174 procapsid structure. Furthermore, application of the, crystallographic 4(1) symmetry operation to one of these dimers generates, a tetramer similar to the tetramer in the icosahedral asymmetric unit of, the procapsid. These data suggest that both dimers and tetramers of the D, protein are true morphogenetic intermediates and can form independently of, other proteins involved in procapsid morphogenesis. The crystal structure, of the D scaffolding protein thus represents the state of the polypeptide, prior to procapsid assembly. Hence, comparison with the procapsid, structure provides a rare opportunity to follow the conformational, switching events necessary for the construction of complex macromolecular, assemblies.
+
<StructureSection load='1tx9' size='340' side='right'caption='[[1tx9]], [[Resolution|resolution]] 3.31&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1tx9]] is a 2 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=1TX9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TX9 FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.31&#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=1tx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tx9 OCA], [https://pdbe.org/1tx9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tx9 RCSB], [https://www.ebi.ac.uk/pdbsum/1tx9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tx9 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[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 ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tx/1tx9_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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=1tx9 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The three-dimensional structure of bacteriophage phiX174 external scaffolding protein D, prior to its interaction with other structural proteins, has been determined to 3.3 angstroms by X-ray crystallography. The crystals belong to space group P4(1)2(1)2 with a dimer in the asymmetric unit that closely resembles asymmetric dimers observed in the phiX174 procapsid structure. Furthermore, application of the crystallographic 4(1) symmetry operation to one of these dimers generates a tetramer similar to the tetramer in the icosahedral asymmetric unit of the procapsid. These data suggest that both dimers and tetramers of the D protein are true morphogenetic intermediates and can form independently of other proteins involved in procapsid morphogenesis. The crystal structure of the D scaffolding protein thus represents the state of the polypeptide prior to procapsid assembly. Hence, comparison with the procapsid structure provides a rare opportunity to follow the conformational switching events necessary for the construction of complex macromolecular assemblies.
-
==About this Structure==
+
Conformational switching by the scaffolding protein D directs the assembly of bacteriophage phiX174.,Morais MC, Fisher M, Kanamaru S, Przybyla L, Burgner J, Fane BA, Rossmann MG Mol Cell. 2004 Sep 24;15(6):991-7. PMID:15383287<ref>PMID:15383287</ref>
-
1TX9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_phix174 Enterobacteria phage phix174]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TX9 OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Conformational switching by the scaffolding protein D directs the assembly of bacteriophage phiX174., Morais MC, Fisher M, Kanamaru S, Przybyla L, Burgner J, Fane BA, Rossmann MG, Mol Cell. 2004 Sep 24;15(6):991-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15383287 15383287]
+
</div>
-
[[Category: Enterobacteria phage phix174]]
+
<div class="pdbe-citations 1tx9" style="background-color:#fffaf0;"></div>
-
[[Category: Single protein]]
+
== References ==
-
[[Category: Fane, B.A.]]
+
<references/>
-
[[Category: Fisher, M.]]
+
__TOC__
-
[[Category: Kanamaru, K.]]
+
</StructureSection>
-
[[Category: Morais, M.C.]]
+
[[Category: Escherichia virus phiX174]]
-
[[Category: Rossmann, M.G.]]
+
[[Category: Large Structures]]
-
[[Category: assembly]]
+
[[Category: Fane BA]]
-
[[Category: conformational switching]]
+
[[Category: Fisher M]]
-
[[Category: phix174]]
+
[[Category: Kanamaru K]]
-
[[Category: scaffolding protein]]
+
[[Category: Morais MC]]
-
 
+
[[Category: Rossmann MG]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:39:52 2007''
+

Current revision

gpd prior to capsid assembly

PDB ID 1tx9

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1tx9"
Personal tools