1ql2: Difference between revisions
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<StructureSection load='1ql2' size='340' side='right' caption='[[1ql2]], [[Resolution|resolution]] 3.10Å' scene=''> | <StructureSection load='1ql2' size='340' side='right' caption='[[1ql2]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ql2]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1ql2]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Bppf1 Bppf1]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QL2 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ql1|1ql1]], [[2ifm|2ifm]], [[2ifn|2ifn]], [[3ifm|3ifm]], [[4ifm|4ifm]], [[1pfi|1pfi]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ql1|1ql1]], [[2ifm|2ifm]], [[2ifn|2ifn]], [[3ifm|3ifm]], [[4ifm|4ifm]], [[1pfi|1pfi]]</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=1ql2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ql2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ql2 RCSB], [http://www.ebi.ac.uk/pdbsum/1ql2 PDBsum]</span></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=1ql2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ql2 OCA], [http://pdbe.org/1ql2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ql2 RCSB], [http://www.ebi.ac.uk/pdbsum/1ql2 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1ql2" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bppf1]] | ||
[[Category: Marvin, D A]] | [[Category: Marvin, D A]] | ||
[[Category: Symmons, M F]] | [[Category: Symmons, M F]] | ||
Revision as of 00:47, 10 September 2015
INOVIRUS (FILAMENTOUS BACTERIOPHAGE) STRAIN PF1 MAJOR COAT PROTEIN ASSEMBLYINOVIRUS (FILAMENTOUS BACTERIOPHAGE) STRAIN PF1 MAJOR COAT PROTEIN ASSEMBLY
Structural highlights
Function[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). Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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