1cd3
From Proteopedia
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| - | [[Image:1cd3.gif|left|200px]] | + | [[Image:1cd3.gif|left|200px]] |
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| - | '''PROCAPSID OF BACTERIOPHAGE PHIX174''' | + | {{Structure |
| + | |PDB= 1cd3 |SIZE=350|CAPTION= <scene name='initialview01'>1cd3</scene>, resolution 3.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''PROCAPSID OF BACTERIOPHAGE PHIX174''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CD3 is a [ | + | 1CD3 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Enterobacteria_phage_phix174 Enterobacteria phage phix174]. The following page contains interesting information on the relation of 1CD3 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb2_1.html Bacteriophage phiX174]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CD3 OCA]. |
==Reference== | ==Reference== | ||
| - | The role of scaffolding proteins in the assembly of the small, single-stranded DNA virus phiX174., Dokland T, Bernal RA, Burch A, Pletnev S, Fane BA, Rossmann MG, J Mol Biol. 1999 May 14;288(4):595-608. PMID:[http:// | + | The role of scaffolding proteins in the assembly of the small, single-stranded DNA virus phiX174., Dokland T, Bernal RA, Burch A, Pletnev S, Fane BA, Rossmann MG, J Mol Biol. 1999 May 14;288(4):595-608. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10329166 10329166] |
[[Category: Bacteriophage phiX174]] | [[Category: Bacteriophage phiX174]] | ||
[[Category: Enterobacteria phage phix174]] | [[Category: Enterobacteria phage phix174]] | ||
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[[Category: scaffolding protein]] | [[Category: scaffolding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:22:54 2008'' |
Revision as of 08:22, 20 March 2008
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PROCAPSID OF BACTERIOPHAGE PHIX174
Overview
An empty precursor particle called the procapsid is formed during assembly of the single-stranded DNA bacteriophage phiX174. Assembly of the phiX174 procapsid requires the presence of the two scaffolding proteins, D and B, which are structural components of the procapsid, but are not found in the mature virion. The X-ray crystallographic structure of a "closed" procapsid particle has been determined to 3.5 A resolution. This structure has an external scaffold made from 240 copies of protein D, 60 copies of the internally located B protein, and contains 60 copies of each of the viral structural proteins F and G, which comprise the shell and the 5-fold spikes, respectively. The F capsid protein has a similar conformation to that seen in the mature virion, and differs from the previously determined 25 A resolution electron microscopic reconstruction of the "open" procapsid, in which the F protein has a different conformation. The D scaffolding protein has a predominantly alpha-helical fold and displays remarkable conformational variability. We report here an improved and refined structure of the closed procapsid and describe in some detail the differences between the four independent D scaffolding proteins per icosahedral asymmetric unit, as well as their interaction with the F capsid protein. We re-analyze and correct the comparison of the closed procapsid with the previously determined cryo-electron microscopic image reconstruction of the open procapsid and discuss the major structural rearrangements that must occur during assembly. A model is proposed in which the D proteins direct the assembly process by sequential binding and conformational switching.
About this Structure
1CD3 is a Protein complex structure of sequences from Enterobacteria phage phix174. The following page contains interesting information on the relation of 1CD3 with [Bacteriophage phiX174]. Full crystallographic information is available from OCA.
Reference
The role of scaffolding proteins in the assembly of the small, single-stranded DNA virus phiX174., Dokland T, Bernal RA, Burch A, Pletnev S, Fane BA, Rossmann MG, J Mol Biol. 1999 May 14;288(4):595-608. PMID:10329166
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