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5vm7

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Revision as of 22:10, 10 April 2020

Pseudo-atomic model of the MurA-A2 complex

5vm7, resolution 5.70Å

Structural highlights

5vm7 is a 2 chain structure with sequence from Allolevivirus subgroup iii and Eco24. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	5vly, 5vlz
Activity:	UDP-N-acetylglucosamine 1-carboxyvinyltransferase, with EC number 2.5.1.7
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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] [MURA_ECO24] Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.

Publication Abstract from PubMed

In single-stranded RNA bacteriophages (ssRNA phages) a single copy of the maturation protein binds the genomic RNA (gRNA) and is required for attachment of the phage to the host pilus. For the canonical Allolevivirus Qbeta the maturation protein, A2, has an additional role as the lysis protein, by its ability to bind and inhibit MurA, which is involved in peptidoglycan biosynthesis. Here, we determined structures of Qbeta virions, virus-like particles, and the Qbeta-MurA complex using single-particle cryoelectron microscopy, at 4.7-A, 3.3-A, and 6.1-A resolutions, respectively. We identified the outer surface of the beta-region in A2 as the MurA-binding interface. Moreover, the pattern of MurA mutations that block Qbeta lysis and the conformational changes of MurA that facilitate A2 binding were found to be due to the intimate fit between A2 and the region encompassing the closed catalytic cleft of substrate-liganded MurA. Additionally, by comparing the Qbeta virion with Qbeta virus-like particles that lack a maturation protein, we observed a structural rearrangement in the capsid coat proteins that is required to package the viral gRNA in its dominant conformation. Unexpectedly, we found a coat protein dimer sequestered in the interior of the virion. This coat protein dimer binds to the gRNA and interacts with the buried alpha-region of A2, suggesting that it is sequestered during the early stage of capsid formation to promote the gRNA condensation required for genome packaging. These internalized coat proteins are the most asymmetrically arranged major capsid proteins yet observed in virus structures.

Structures of Qbeta virions, virus-like particles, and the Qbeta-MurA complex reveal internal coat proteins and the mechanism of host lysis.,Cui Z, Gorzelnik KV, Chang JY, Langlais C, Jakana J, Young R, Zhang J Proc Natl Acad Sci U S A. 2017 Oct 31;114(44):11697-11702. doi:, 10.1073/pnas.1707102114. Epub 2017 Oct 16. PMID:29078304^[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
↑ Cui Z, Gorzelnik KV, Chang JY, Langlais C, Jakana J, Young R, Zhang J. Structures of Qbeta virions, virus-like particles, and the Qbeta-MurA complex reveal internal coat proteins and the mechanism of host lysis. Proc Natl Acad Sci U S A. 2017 Oct 31;114(44):11697-11702. doi:, 10.1073/pnas.1707102114. Epub 2017 Oct 16. PMID:29078304 doi:http://dx.doi.org/10.1073/pnas.1707102114

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5vm7"

@@ Line 3: / Line 3: @@
 <SX load='5vm7' size='340' side='right' viewer='molstar' caption='[[5vm7]], [[Resolution|resolution]] 5.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5vm7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Allolevivirus_subgroup_iii Allolevivirus subgroup iii] and [http://en.wikipedia.org/wiki/Eco24 Eco24]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VM7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VM7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5vm7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Allolevivirus_subgroup_iii Allolevivirus subgroup iii] and [http://en.wikipedia.org/wiki/Eco24 Eco24]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VM7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5VM7 FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5vly|5vly]], [[5vlz|5vlz]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_1-carboxyvinyltransferase UDP-N-acetylglucosamine 1-carboxyvinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.7 2.5.1.7] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5vm7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vm7 OCA], [http://pdbe.org/5vm7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vm7 RCSB], [http://www.ebi.ac.uk/pdbsum/5vm7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vm7 ProSAT]</span></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=5vm7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vm7 OCA], [http://pdbe.org/5vm7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vm7 RCSB], [http://www.ebi.ac.uk/pdbsum/5vm7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vm7 ProSAT]</span></td></tr>
 </table>
 == Function ==

5vm7

From Proteopedia

Revision as of 22:10, 10 April 2020

Pseudo-atomic model of the MurA-A2 complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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