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5UU5

Bacteriophage P22 mature virion capsid protein

Summary for 5UU5
Entry DOI10.2210/pdb5uu5/pdb
Related2XYZ
EMDB information1826 8606
DescriptorMajor capsid protein (1 entity in total)
Functional Keywordsp22 bacteriophage, virus
Biological sourceSalmonella phage P22 (Enterobacteria phage P22)
Total number of polymer chains7
Total formula weight327569.29
Authors
Hryc, C.F.,Chen, D.-H.,Afonine, P.V.,Jakana, J.,Wang, Z.,Haase-Pettingell, C.,Jiang, W.,Adams, P.D.,King, J.A.,Schmid, M.F.,Chiu, W. (deposition date: 2017-02-16, release date: 2017-03-15, Last modification date: 2024-03-13)
Primary citationHryc, C.F.,Chen, D.H.,Afonine, P.V.,Jakana, J.,Wang, Z.,Haase-Pettingell, C.,Jiang, W.,Adams, P.D.,King, J.A.,Schmid, M.F.,Chiu, W.
Accurate model annotation of a near-atomic resolution cryo-EM map.
Proc. Natl. Acad. Sci. U.S.A., 114:3103-3108, 2017
Cited by
PubMed Abstract: Electron cryomicroscopy (cryo-EM) has been used to determine the atomic coordinates (models) from density maps of biological assemblies. These models can be assessed by their overall fit to the experimental data and stereochemical information. However, these models do not annotate the actual density values of the atoms nor their positional uncertainty. Here, we introduce a computational procedure to derive an atomic model from a cryo-EM map with annotated metadata. The accuracy of such a model is validated by a faithful replication of the experimental cryo-EM map computed using the coordinates and associated metadata. The functional interpretation of any structural features in the model and its utilization for future studies can be made in the context of its measure of uncertainty. We applied this protocol to the 3.3-Å map of the mature P22 bacteriophage capsid, a large and complex macromolecular assembly. With this protocol, we identify and annotate previously undescribed molecular interactions between capsid subunits that are crucial to maintain stability in the absence of cementing proteins or cross-linking, as occur in other bacteriophages.
PubMed: 28270620
DOI: 10.1073/pnas.1621152114
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.3 Å)
Structure validation

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