1ql1: Difference between revisions

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-[[Image:1ql1.gif|left|200px]]<br /><applet load="1ql1" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1ql1, 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='1ql1' size='340' side='right'caption='[[1ql1]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1ql1]] is a 1 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=1QL1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QL1 FirstGlance]. <br>
+</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=1ql1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ql1 OCA], [https://pdbe.org/1ql1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ql1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ql1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ql1 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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).
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-==About this Structure==
+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:10666593<ref>PMID:10666593</ref>
-QL1 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=1QL1 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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]
+</div>
-[[Category: Pseudomonas phage pf1]]
+<div class="pdbe-citations 1ql1" style="background-color:#fffaf0;"></div>
-[[Category: Single protein]]
+== References ==
-[[Category: Marvin, D.A.]]
+<references/>
-[[Category: Symmons, M.F.]]
+__TOC__
-[[Category: Welsh, L.C.]]
+</StructureSection>
-[[Category: helical virus]]
+[[Category: Large Structures]]
-[[Category: helical virus coat protein]]
+[[Category: Pseudomonas virus Pf1]]
-[[Category: inovirus]]
+[[Category: Marvin DA]]
-[[Category: ssdna viruses]]
+[[Category: Symmons MF]]
+[[Category: Welsh LC]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:47:10 2007''