6pxe

From Proteopedia

(Difference between revisions)

Revision as of 09:58, 12 August 2020

Crystal structure of the complex between periplasmic domains of antiholin RI and holin T from T4 phage, in P21

Structural highlights

6pxe is a 8 chain structure with sequence from Bpt4 and Escherichia phage vb_ecom_nbg2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	rI, 58.6, rIA, tk.-2 (BPT4), vBEcoMNBG2_239 (Escherichia phage vB_EcoM_NBG2)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ANTIH_BPT4] Involved in lysis inhibition. Interacts with and inhibits the holin thereby delaying the host cell lysis timing. Lysis inhibition is imposed when a cell infected by a T4-like virus is superinfected by new incoming viruses. This is probably due to the capsid content of the new phage being released in the periplasm because of blockage of entry due to superinfection exclusion. These periplasmically released viral proteins must somehow activate the periplasmic antiholin, which in turn will block the holin multimerization.[HAMAP-Rule:MF_04105]^[1] ^[2] ^[3] [A0A2U8QQK7_9CAUD] Accumulates harmlessly in the cytoplasmic membrane until it reaches a critical concentration that triggers the formation of micron-scale pores (holes) causing host cell membrane disruption and endolysin escape into the periplasmic space. Determines the precise timing of host cell lysis. Participates with the endolysin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles from the host cell.[HAMAP-Rule:MF_04104]

Publication Abstract from PubMed

Optimal phage propagation depends on the regulation of the lysis of the infected host cell. In T4 phage infection, lysis occurs when the holin protein (T) forms lesions in the host membrane. However, the lethal function of T can be blocked by an antiholin (RI) during lysis inhibition (LIN). LIN sets if the infected cell undergoes superinfection, then the lysis is delayed until host/phage ratio becomes more favorable for the release of progeny. It has been thought that a signal derived from the superinfection is required to activate RI. Here we report structures that suggest a radically different model in which RI binds to T irrespective of superinfection, causing it to accumulate in a membrane as heterotetrameric 2RI-2T complex. Moreover, we show the complex binds non-specifically to DNA, suggesting that the gDNA from the superinfecting phage serves as the LIN signal and that stabilization of the complex by DNA binding is what defines LIN. Finally, we show that soluble domain of free RI crystallizes in a domain-swapped homotetramer, which likely works as a sink for RI molecules released from the RI-T complex to ensure efficient lysis. These results constitute the first structural basis and a new model not only for the historic LIN phenomenon but also for the temporal regulation of phage lysis in general.

The Structural Basis of T4 Phage Lysis Control: DNA as the Signal for Lysis Inhibition.,Krieger I, Kuznetsov V, Chang JY, Zhang J, Moussa S, Young R, Sacchettini JC J Mol Biol. 2020 Jun 17. pii: S0022-2836(20)30409-5. doi:, 10.1016/j.jmb.2020.06.013. PMID:32562709^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Tran TA, Struck DK, Young R. The T4 RI antiholin has an N-terminal signal anchor release domain that targets it for degradation by DegP. J Bacteriol. 2007 Nov;189(21):7618-25. doi: 10.1128/JB.00854-07. Epub 2007 Aug, 10. PMID:17693511 doi:http://dx.doi.org/10.1128/JB.00854-07
↑ Moussa SH, Kuznetsov V, Tran TA, Sacchettini JC, Young R. Protein determinants of phage T4 lysis inhibition. Protein Sci. 2012 Apr;21(4):571-82. doi: 10.1002/pro.2042. Epub 2012 Mar 2. PMID:22389108 doi:http://dx.doi.org/10.1002/pro.2042
↑ Paddison P, Abedon ST, Dressman HK, Gailbreath K, Tracy J, Mosser E, Neitzel J, Guttman B, Kutter E. The roles of the bacteriophage T4 r genes in lysis inhibition and fine-structure genetics: a new perspective. Genetics. 1998 Apr;148(4):1539-50. PMID:9560373
↑ Krieger I, Kuznetsov V, Chang JY, Zhang J, Moussa S, Young R, Sacchettini JC. The Structural Basis of T4 Phage Lysis Control: DNA as the Signal for Lysis Inhibition. J Mol Biol. 2020 Jun 17. pii: S0022-2836(20)30409-5. doi:, 10.1016/j.jmb.2020.06.013. PMID:32562709 doi:http://dx.doi.org/10.1016/j.jmb.2020.06.013

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6pxe"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the complex between periplasmic domains of antiholin RI and holin T from T4 phage, in P21==
-<StructureSection load='6pxe' size='340' side='right'caption='[[6pxe]]' scene=''>
+<StructureSection load='6pxe' size='340' side='right'caption='[[6pxe]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PXE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6PXE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6pxe]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4] and [http://en.wikipedia.org/wiki/Escherichia_phage_vb_ecom_nbg2 Escherichia phage vb_ecom_nbg2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PXE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6PXE 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=6pxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pxe OCA], [http://pdbe.org/6pxe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pxe RCSB], [http://www.ebi.ac.uk/pdbsum/6pxe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pxe ProSAT]</span></td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rI, 58.6, rIA, tk.-2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4]), vBEcoMNBG2_239 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2184699 Escherichia phage vB_EcoM_NBG2])</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=6pxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pxe OCA], [http://pdbe.org/6pxe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pxe RCSB], [http://www.ebi.ac.uk/pdbsum/6pxe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pxe ProSAT]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/ANTIH_BPT4 ANTIH_BPT4]] Involved in lysis inhibition. Interacts with and inhibits the holin thereby delaying the host cell lysis timing. Lysis inhibition is imposed when a cell infected by a T4-like virus is superinfected by new incoming viruses. This is probably due to the capsid content of the new phage being released in the periplasm because of blockage of entry due to superinfection exclusion. These periplasmically released viral proteins must somehow activate the periplasmic antiholin, which in turn will block the holin multimerization.[HAMAP-Rule:MF_04105]<ref>PMID:17693511</ref> <ref>PMID:22389108</ref> <ref>PMID:9560373</ref>  [[http://www.uniprot.org/uniprot/A0A2U8QQK7_9CAUD A0A2U8QQK7_9CAUD]] Accumulates harmlessly in the cytoplasmic membrane until it reaches a critical concentration that triggers the formation of micron-scale pores (holes) causing host cell membrane disruption and endolysin escape into the periplasmic space. Determines the precise timing of host cell lysis. Participates with the endolysin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles from the host cell.[HAMAP-Rule:MF_04104]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Optimal phage propagation depends on the regulation of the lysis of the infected host cell. In T4 phage infection, lysis occurs when the holin protein (T) forms lesions in the host membrane. However, the lethal function of T can be blocked by an antiholin (RI) during lysis inhibition (LIN). LIN sets if the infected cell undergoes superinfection, then the lysis is delayed until host/phage ratio becomes more favorable for the release of progeny. It has been thought that a signal derived from the superinfection is required to activate RI. Here we report structures that suggest a radically different model in which RI binds to T irrespective of superinfection, causing it to accumulate in a membrane as heterotetrameric 2RI-2T complex. Moreover, we show the complex binds non-specifically to DNA, suggesting that the gDNA from the superinfecting phage serves as the LIN signal and that stabilization of the complex by DNA binding is what defines LIN. Finally, we show that soluble domain of free RI crystallizes in a domain-swapped homotetramer, which likely works as a sink for RI molecules released from the RI-T complex to ensure efficient lysis. These results constitute the first structural basis and a new model not only for the historic LIN phenomenon but also for the temporal regulation of phage lysis in general.
+The Structural Basis of T4 Phage Lysis Control: DNA as the Signal for Lysis Inhibition.,Krieger I, Kuznetsov V, Chang JY, Zhang J, Moussa S, Young R, Sacchettini JC J Mol Biol. 2020 Jun 17. pii: S0022-2836(20)30409-5. doi:, 10.1016/j.jmb.2020.06.013. PMID:32562709<ref>PMID:32562709</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 6pxe" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>
+[[Category: Bpt4]]
+[[Category: Escherichia phage vb_ecom_nbg2]]
 [[Category: Large Structures]]
-[[Category: Krieger IV]]
+[[Category: Krieger, I V]]
-[[Category: Sacchettini JC]]
+[[Category: Sacchettini, J C]]
+[[Category: Lysis inhibition]]
+[[Category: Phage]]
+[[Category: Viral protein]]

6pxe

From Proteopedia

Revision as of 09:58, 12 August 2020

Crystal structure of the complex between periplasmic domains of antiholin RI and holin T from T4 phage, in P21

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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