1ql2: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
New page: left|200px<br /><applet load="1ql2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ql2, resolution 3.1Å" /> '''INOVIRUS (FILAMENTOUS...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
(15 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1ql2.gif|left|200px]]<br /><applet load="1ql2" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ql2, resolution 3.1&Aring;" />
'''INOVIRUS (FILAMENTOUS BACTERIOPHAGE) STRAIN PF1 MAJOR COAT PROTEIN ASSEMBLY'''<br />


==Overview==
==Inovirus (Filamentous Bacteriophage) Strain PF1 Major Coat Protein Assembly==
The major coat protein in the capsid of Pf1 filamentous bacteriophage, (Inovirus) forms a helical assembly of about 7000 identical protein, subunits, each of which contains 46 amino-acid residues and can be closely, approximated by a single gently curved alpha-helix. Since the viral DNA, occupies the core of the tubular capsid and appears to make no significant, specific interactions with the capsid proteins, the capsid is a simple, model system for the study of the static and dynamic properties of, alpha-helix assembly. The capsid undergoes a reversible, temperature-induced structural transition at about 283 K between two, slightly different helix forms. The two forms can coexist without an, intermediate state, consistent with a first-order structural phase, transition. The molecular model of the higher temperature form was refined, using improved X-ray fibre diffraction data and new refinement and, validation methods. The refinement indicates that the two forms are, related by a change in the orientation of the capsid subunits within the, virion, without a significant change in local conformation of the, subunits. On the higher temperature diffraction pattern there is a region, of observed intensity that is not consistent with a simple helix of, identical subunits; it is proposed that the structure involves groups of, three subunits which each have a slightly different orientation within the, group. The grouping of subunits suggests that a change in subunit, libration frequency could be the basis of the Pf1 structural transition;, calculations from the model are used to explore this idea.
<StructureSection load='1ql2' size='340' side='right'caption='[[1ql2]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1ql2]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_virus_Pf1 Pseudomonas virus Pf1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QL2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QL2 FirstGlance]. <br>
1QL2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_phage_pf1 Pseudomonas phage pf1]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QL2 OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Fiber diffraction, [[Resolution|Resolution]] 3.1&#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=1ql2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ql2 OCA], [https://pdbe.org/1ql2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ql2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ql2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ql2 ProSAT]</span></td></tr>
==Reference==
</table>
The molecular structure and structural transition of the alpha-helical capsid in filamentous bacteriophage Pf1., Welsh LC, Symmons MF, Marvin DA, Acta Crystallogr D Biol Crystallogr. 2000 Feb;56(Pt 2):137-50. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10666593 10666593]
== Function ==
[[Category: Pseudomonas phage pf1]]
[https://www.uniprot.org/uniprot/CAPSD_BPPF1 CAPSD_BPPF1] Self assembles to form a helical capsid wrapping up the viral genomic DNA. The capsid displays a filamentous structure with a length of 760-1950 nm and a width of 6-8 nm. The virion assembly and budding take place at the host inner membrane (By similarity).
[[Category: Single protein]]
__TOC__
[[Category: Marvin, D.A.]]
</StructureSection>
[[Category: Symmons, M.F.]]
[[Category: Large Structures]]
[[Category: Welsh, L.C.]]
[[Category: Pseudomonas virus Pf1]]
[[Category: helical virus]]
[[Category: Marvin DA]]
[[Category: helical virus coat protein]]
[[Category: Symmons MF]]
[[Category: inovirus]]
[[Category: Welsh LC]]
[[Category: ssdna viruses]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:47:14 2007''

Latest revision as of 08:15, 14 February 2024

Inovirus (Filamentous Bacteriophage) Strain PF1 Major Coat Protein Assembly

1ql2, resolution 3.10Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1ql2&oldid=4053831"