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5GAI

Probabilistic Structural Models of Mature P22 Bacteriophage Portal, Hub, and Tailspike proteins

Summary for 5GAI
Entry DOI10.2210/pdb5gai/pdb
EMDB information5348 8005
DescriptorPortal protein, Peptidoglycan hydrolase gp4, Tail fiber protein (3 entities in total)
Functional Keywordsvirion, portal, tailspike, adhesin, viral protein
Biological sourceEnterobacteria phage P22
More
Total number of polymer chains27
Total formula weight1394354.25
Authors
Pintilie, G.,Chen, D.H.,Haase-Pettingell, C.A.,King, J.A.,Chiu, W. (deposition date: 2015-12-01, release date: 2016-02-17, Last modification date: 2024-03-06)
Primary citationPintilie, G.,Chen, D.H.,Haase-Pettingell, C.A.,King, J.A.,Chiu, W.
Resolution and Probabilistic Models of Components in CryoEM Maps of Mature P22 Bacteriophage.
Biophys.J., 110:827-839, 2016
Cited by
PubMed Abstract: CryoEM continues to produce density maps of larger and more complex assemblies with multiple protein components of mixed symmetries. Resolution is not always uniform throughout a cryoEM map, and it can be useful to estimate the resolution in specific molecular components of a large assembly. In this study, we present procedures to 1) estimate the resolution in subcomponents by gold-standard Fourier shell correlation (FSC); 2) validate modeling procedures, particularly at medium resolutions, which can include loop modeling and flexible fitting; and 3) build probabilistic models that combine high-accuracy priors (such as crystallographic structures) with medium-resolution cryoEM densities. As an example, we apply these methods to new cryoEM maps of the mature bacteriophage P22, reconstructed without imposing icosahedral symmetry. Resolution estimates based on gold-standard FSC show the highest resolution in the coat region (7.6 Å), whereas other components are at slightly lower resolutions: portal (9.2 Å), hub (8.5 Å), tailspike (10.9 Å), and needle (10.5 Å). These differences are indicative of inherent structural heterogeneity and/or reconstruction accuracy in different subcomponents of the map. Probabilistic models for these subcomponents provide new insights, to our knowledge, and structural information when taking into account uncertainty given the limitations of the observed density.
PubMed: 26743049
DOI: 10.1016/j.bpj.2015.11.3522
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (10.5 Å)
Structure validation

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