2c0w

From Proteopedia

(Difference between revisions)

Revision as of 10:24, 6 September 2023

Molecular Structure of fd Filamentous Bacteriophage Refined with Respect to X-ray Fibre Diffraction

Structural highlights

2c0w is a 1 chain structure with sequence from Enterobacteria phage fd. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Fiber diffraction, Resolution 3.2Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CAPSD_BPFD 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 PubMed

Filamentous bacteriophage (Inovirus) is a simple and well-characterized model system. The phage particle, or virion, is about 60 angstroms in diameter and several thousand angstrom units long. The virions are assembled at the bacterial membrane as they extrude out of the host without killing it, an example of specific transport of nucleoprotein assemblages across membranes. The Ff group (fd, f1 and M13) has been especially widely studied. Models of virion assembly have been proposed based on a molecular model of the fd virion derived by X-ray fibre diffraction. A somewhat different model of the fd virion using solid-state NMR data has been proposed, not consistent with these models of assembly nor with the X-ray diffraction data. Here we show that reinterpreted NMR data are also consistent with the model derived from X-ray fibre diffraction studies, and discuss models of virion assembly.

Molecular structure of fd (f1, M13) filamentous bacteriophage refined with respect to X-ray fibre diffraction and solid-state NMR data supports specific models of phage assembly at the bacterial membrane.,Marvin DA, Welsh LC, Symmons MF, Scott WR, Straus SK J Mol Biol. 2006 Jan 13;355(2):294-309. Epub 2005 Nov 8. PMID:16300790^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Marvin DA, Welsh LC, Symmons MF, Scott WR, Straus SK. Molecular structure of fd (f1, M13) filamentous bacteriophage refined with respect to X-ray fibre diffraction and solid-state NMR data supports specific models of phage assembly at the bacterial membrane. J Mol Biol. 2006 Jan 13;355(2):294-309. Epub 2005 Nov 8. PMID:16300790 doi:10.1016/j.jmb.2005.10.048

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2c0w"

@@ Line 3: / Line 3: @@
 <StructureSection load='2c0w' size='340' side='right'caption='[[2c0w]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2c0w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpfd Bpfd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C0W FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2c0w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacteria_phage_fd Enterobacteria phage fd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C0W FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2c0x|2c0x]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Fiber diffraction, [[Resolution|Resolution]] 3.2&#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=2c0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c0w OCA], [https://pdbe.org/2c0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c0w RCSB], [https://www.ebi.ac.uk/pdbsum/2c0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c0w ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/CAPSD_BPFD CAPSD_BPFD]] 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).
+[https://www.uniprot.org/uniprot/CAPSD_BPFD CAPSD_BPFD] 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 ==
@@ Line 22: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Bpfd]]
+[[Category: Enterobacteria phage fd]]
 [[Category: Large Structures]]
-[[Category: Marvin, D A]]
+[[Category: Marvin DA]]
-[[Category: Scott, W R.P]]
+[[Category: Scott WRP]]
-[[Category: Straus, S K]]
+[[Category: Straus SK]]
-[[Category: Symmons, M F]]
+[[Category: Symmons MF]]
-[[Category: Welsh, L C]]
+[[Category: Welsh LC]]
-[[Category: Capsid protein]]
-[[Category: Filamentous bacteriophage]]
-[[Category: Helical virus]]
-[[Category: Membrane protein]]
-[[Category: Structural protein]]
-[[Category: Virus]]

2c0w

From Proteopedia

Revision as of 10:24, 6 September 2023

Molecular Structure of fd Filamentous Bacteriophage Refined with Respect to X-ray Fibre Diffraction

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox