4itv

Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains, triple mutant, P212121 form

spinqualitylabelsall models 4itv, resolution 3.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4itv is a 12 chain structure with sequence from Influenza A virus (A/Puerto Rico/8/1934(H1N1)) and Kitasatospora aureofaciens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.598Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BPOA2_KITAU May be a chlorinating enzyme involved in 7-chlorotetracycline biosynthesis.M1_I34A1 Plays critical roles in virus replication, from virus entry and uncoating to assembly and budding of the virus particle. M1 binding to ribonucleocapsids (RNPs) in nucleus seems to inhibit viral transcription. Interaction of viral NEP with M1-RNP is thought to promote nuclear export of the complex, which is targeted to the virion assembly site at the apical plasma membrane in polarized epithelial cells. Interactions with NA and HA may bring M1, a non-raft-associated protein, into lipid rafts. Forms a continuous shell on the inner side of the lipid bilayer in virion, where it binds the RNP. During virus entry into cell, the M2 ion channel acidifies the internal virion core, inducing M1 dissociation from the RNP. M1-free RNPs are transported to the nucleus, where viral transcription and replication can take place. Determines the virion's shape: spherical or filamentous. Clinical isolates of influenza are characterized by the presence of significant proportion of filamentous virions, whereas after multiple passage on eggs or cell culture, virions have only spherical morphology. Filamentous virions are thought to be important to infect neighboring cells, and spherical virions more suited to spread through aerosol between hosts organisms. Publication Abstract from PubMed Designing protein molecules that self-assemble into complex architectures is an outstanding goal in the area of nanobiotechnology. One design strategy for doing this involves genetically fusing together two natural proteins, each of which is known to form a simple oligomer on its own (e.g., a dimer or trimer). If two such components can be fused in a geometrically predefined configuration, that designed subunit can, in principle, assemble into highly symmetric architectures. Initial experiments showed that a 12-subunit tetrahedral cage, 16 nm in diameter, could be constructed following such a procedure [Padilla, J. E.; et al. Proc. Natl. Acad. Sci. U.S.A. 2001, 98, 2217; Lai, Y. T.; et al. Science 2012, 336, 1129]. Here we characterize multiple crystal structures of protein cages constructed in this way, including cages assembled from two mutant forms of the same basic protein subunit. The flexibilities of the designed assemblies and their deviations from the target model are described, along with implications for further design developments. Structure and flexibility of nanoscale protein cages designed by symmetric self-assembly.,Lai YT, Tsai KL, Sawaya MR, Asturias FJ, Yeates TO J Am Chem Soc. 2013 May 22;135(20):7738-43. doi: 10.1021/ja402277f. Epub 2013 May, 8. PMID:23621606 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Haloperoxidase

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