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| | <StructureSection load='5mnt' size='340' side='right'caption='[[5mnt]], [[Resolution|resolution]] 3.32Å' scene=''> | | <StructureSection load='5mnt' size='340' side='right'caption='[[5mnt]], [[Resolution|resolution]] 3.32Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5mnt]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Allolevivirus_subgroup_iii Allolevivirus subgroup iii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MNT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5MNT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5mnt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_Qbeta Escherichia virus Qbeta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MNT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MNT FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5mnt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mnt OCA], [http://pdbe.org/5mnt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mnt RCSB], [http://www.ebi.ac.uk/pdbsum/5mnt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mnt ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.32Å</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5mnt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mnt OCA], [https://pdbe.org/5mnt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mnt RCSB], [https://www.ebi.ac.uk/pdbsum/5mnt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mnt ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/MATA2_BPQBE MATA2_BPQBE] Induces host cell lysis (PubMed:11892805). Inhibits host MurA activity thereby blocking the synthesis of murein precursors necessary for the host cell wall biosynthesis (PubMed:11423662). May be responsible for the attachment to the host pilus. Makes extensive contacts with the viral genome (PubMed:28111107).<ref>PMID:11423662</ref> <ref>PMID:11892805</ref> <ref>PMID:23329676</ref> <ref>PMID:28111107</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Allolevivirus subgroup iii]] | + | [[Category: Escherichia virus Qbeta]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Rumnieks, J]] | + | [[Category: Rumnieks J]] |
| - | [[Category: Tars, K]] | + | [[Category: Tars K]] |
| - | [[Category: Minor capsid protein]]
| + | |
| - | [[Category: Rna binding protein]]
| + | |
| - | [[Category: Virus attachment]]
| + | |
| Structural highlights
Function
MATA2_BPQBE Induces host cell lysis (PubMed:11892805). Inhibits host MurA activity thereby blocking the synthesis of murein precursors necessary for the host cell wall biosynthesis (PubMed:11423662). May be responsible for the attachment to the host pilus. Makes extensive contacts with the viral genome (PubMed:28111107).[1] [2] [3] [4]
Publication Abstract from PubMed
Virions of the single-stranded RNA bacteriophages contain a single copy of the maturation protein, which is bound to the phage genome and is required for the infectivity of the particles. The maturation protein mediates the adsorption of the virion to bacterial pili and the subsequent release and penetration of the genome into the host cell. Here, we report a crystal structure of the maturation protein from bacteriophage Qbeta. The protein has a bent, highly asymmetric shape and spans 110A in length. Apart from small local substructures, the overall fold of the maturation protein does not resemble that of other known proteins. The protein is organized in two distinct regions, an alpha-helical part with a four-helix core, and a beta stranded part that contains a seven-stranded sheet in the central part and a five-stranded sheet at the tip of the protein. The Qbeta maturation protein has two distinct, positively charged areas at opposite sides of the alpha-helical part, which are involved in genomic RNA binding. The maturation protein binds to each of the surrounding coat protein dimers in the capsid differently, and the interaction is considerably weaker compared to coat protein interdimer contacts. The coat protein- or RNA-binding residues are not preserved among different ssRNA phage maturation proteins; instead, the distal end of the alpha-helical part is the most evolutionarily conserved, suggesting the importance of this region for maintaining the functionality of the protein.
Crystal Structure of the Maturation Protein from Bacteriophage Qbeta.,Rumnieks J, Tars K J Mol Biol. 2017 Jan 19. pii: S0022-2836(17)30040-2. doi:, 10.1016/j.jmb.2017.01.012. PMID:28111107[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bernhardt TG, Wang IN, Struck DK, Young R. A protein antibiotic in the phage Qbeta virion: diversity in lysis targets. Science. 2001 Jun 22;292(5525):2326-9. PMID:11423662 doi:http://dx.doi.org/10.1126/science.1058289
- ↑ Karnik S, Billeter M. The lysis function of RNA bacteriophage Qbeta is mediated by the maturation (A2) protein. EMBO J. 1983;2(9):1521-6. PMID:11892805
- ↑ Reed CA, Langlais C, Wang IN, Young R. A(2) expression and assembly regulates lysis in Qbeta infections. Microbiology. 2013 Mar;159(Pt 3):507-14. doi: 10.1099/mic.0.064790-0. Epub 2013, Jan 17. PMID:23329676 doi:http://dx.doi.org/10.1099/mic.0.064790-0
- ↑ Rumnieks J, Tars K. Crystal Structure of the Maturation Protein from Bacteriophage Qbeta. J Mol Biol. 2017 Jan 19. pii: S0022-2836(17)30040-2. doi:, 10.1016/j.jmb.2017.01.012. PMID:28111107 doi:http://dx.doi.org/10.1016/j.jmb.2017.01.012
- ↑ Rumnieks J, Tars K. Crystal Structure of the Maturation Protein from Bacteriophage Qbeta. J Mol Biol. 2017 Jan 19. pii: S0022-2836(17)30040-2. doi:, 10.1016/j.jmb.2017.01.012. PMID:28111107 doi:http://dx.doi.org/10.1016/j.jmb.2017.01.012
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