Structural highlights
Function
CAPSD_BPPP7 Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 26 nm in diameter, and consisting of 89 capsid proteins dimers (178 capsid proteins) (PubMed:10739912). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome (By similarity).[UniProtKB:P03612][1] Acts as a translational repressor of viral replicase synthesis late in infection. This latter function is the result of capsid protein interaction with an RNA hairpin which contains the replicase ribosome-binding site.[2]
Publication Abstract from PubMed
The structure of bacteriophage PP7 from Pseudomomas aeruginosa was determined to 3.7 A resolution. Triclinic crystals of three forms were obtained, diffracting to between 4.5 and 3.4 A resolution. The quality of the crystals was exceptionally poor, leading to problems in the evaluation of the recorded images and to a final data set which would appear to be useless with standard criteria for protein crystals. In all crystal forms, the unit cell contains two icosahedral particles, providing 120-fold non-crystallographic symmetry. For two of the crystal forms, the particle orientations were calculated using the self-rotation function. The two particles in the asymmetric unit had very similar but distinct orientations. The position of the second particle was found using the Patterson function. Initial phases to 15 A resolution were calculated using the related phage MS2 as a model. Real-space averaging was performed and phases were extended from 15 A resolution to the limit of the data. The map was improved significantly by using only the 'high' resolution data in the resolution range 7-3.7 A, allowing the positions of most side chains to be determined. The better quality of the 7-3.7 A resolution map is presumably a consequence of the presence of satellite crystals. The position of the second particle was improved using the correlation coefficient in the averaging process to monitor the refinement by moving the particle around in small steps.
Structure determination of bacteriophage PP7 from Pseudomonas aeruginosa: from poor data to a good map.,Tars K, Fridborg K, Bundule M, Liljas L Acta Crystallogr D Biol Crystallogr. 2000 Apr;56(Pt 4):398-405. PMID:10739912[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tars K, Fridborg K, Bundule M, Liljas L. Structure determination of bacteriophage PP7 from Pseudomonas aeruginosa: from poor data to a good map. Acta Crystallogr D Biol Crystallogr. 2000 Apr;56(Pt 4):398-405. PMID:10739912
- ↑ Lim F, Downey TP, Peabody DS. Translational repression and specific RNA binding by the coat protein of the Pseudomonas phage PP7. J Biol Chem. 2001 Jun 22;276(25):22507-13. PMID:11306589 doi:10.1074/jbc.M102411200
- ↑ Tars K, Fridborg K, Bundule M, Liljas L. Structure determination of bacteriophage PP7 from Pseudomonas aeruginosa: from poor data to a good map. Acta Crystallogr D Biol Crystallogr. 2000 Apr;56(Pt 4):398-405. PMID:10739912
