6k4y

From Proteopedia

(Difference between revisions)

Revision as of 02:19, 11 April 2020

CryoEM structure of sigma appropriation complex

6k4y, resolution 3.79Å

Structural highlights

6k4y is a 10 chain structure with sequence from Bpt4 and Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	rpoA (ECOLI), rpoB (ECOLI), rpoC (ECOLI), rpoZ (ECOLI), rpoD (ECOLI), asiA (BPT4), motA (BPT4)
Activity:	DNA-directed RNA polymerase, with EC number 2.7.7.6
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ASIA_BPT4] Transcriptional inhibitor. Inhibits sigma 70-directed transcription by weakening its interaction with the core of the host's RNA polymerase. This allows Gp55 to successfully compete for the core enzyme. Plays an important role during the prereplicative period of phage T4 development.^[1] ^[2] [RPOC_ECOLI] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01322] [MOTA_BPT4] Required for the transcriptional activation of middle promoters. Middle promoters are characterized by the presence of the conserved sequence [AT]3TGCTTNA (MotA box). MotA binds directly to MotA boxes. [RPOB_ECOLI] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01321] [RPOA_ECOLI] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme.[HAMAP-Rule:MF_00059] [RPOZ_ECOLI] Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.[HAMAP-Rule:MF_00366] [RPOD_ECOLI] Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This is the primary sigma factor of this bacterium.

Publication Abstract from PubMed

Bacteriophage T4 middle promoters are activated through a process called sigma appropriation, which requires the concerted effort of two T4-encoded transcription factors: AsiA and MotA. Despite extensive biochemical and genetic analyses, puzzle remains, in part, because of a lack of precise structural information for sigma appropriation complex. Here, we report a single-particle cryo-electron microscopy (cryo-EM) structure of an intact sigma appropriation complex, comprising AsiA, MotA, Escherichia coli RNA polymerase (RNAP), sigma70 and a T4 middle promoter. As expected, AsiA binds to and remodels sigma region 4 to prevent its contact with host promoters. Unexpectedly, AsiA undergoes a large conformational change, takes over the job of sigma region 4 and provides an anchor point for the upstream double-stranded DNA. Because sigma region 4 is conserved among bacteria, other transcription factors may use the same strategy to alter the landscape of transcription immediately. Together, the structure provides a foundation for understanding sigma appropriation and transcription activation.

Structural basis of sigma appropriation.,Shi J, Wen A, Zhao M, You L, Zhang Y, Feng Y Nucleic Acids Res. 2019 Aug 8. pii: 5545004. doi: 10.1093/nar/gkz682. PMID:31392983^[3]

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

References

↑ Ouhammouch M, Orsini G, Brody EN. The asiA gene product of bacteriophage T4 is required for middle mode RNA synthesis. J Bacteriol. 1994 Jul;176(13):3956-65. PMID:8021178
↑ Lambert LJ, Wei Y, Schirf V, Demeler B, Werner MH. T4 AsiA blocks DNA recognition by remodeling sigma70 region 4. EMBO J. 2004 Aug 4;23(15):2952-62. Epub 2004 Jul 15. PMID:15257291 doi:10.1038/sj.emboj.7600312
↑ Shi J, Wen A, Zhao M, You L, Zhang Y, Feng Y. Structural basis of sigma appropriation. Nucleic Acids Res. 2019 Aug 8. pii: 5545004. doi: 10.1093/nar/gkz682. PMID:31392983 doi:http://dx.doi.org/10.1093/nar/gkz682

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/6k4y"

@@ Line 3: / Line 3: @@
 <SX load='6k4y' size='340' side='right' viewer='molstar' caption='[[6k4y]], [[Resolution|resolution]] 3.79&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6k4y]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4] and [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K4Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6K4Y FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6k4y]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4] and [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K4Y OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6K4Y FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rpoA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), rpoB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), rpoC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), rpoZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), rpoD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), asiA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4]), motA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] </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=6k4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k4y OCA], [http://pdbe.org/6k4y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k4y RCSB], [http://www.ebi.ac.uk/pdbsum/6k4y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k4y 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=6k4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k4y OCA], [http://pdbe.org/6k4y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k4y RCSB], [http://www.ebi.ac.uk/pdbsum/6k4y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k4y ProSAT]</span></td></tr>
 </table>
 == Function ==

6k4y

From Proteopedia

Revision as of 02:19, 11 April 2020

CryoEM structure of sigma appropriation complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox