1z3e

From Proteopedia

(Difference between revisions)

Revision as of 16:12, 12 October 2017

Crystal Structure of Spx in Complex with the C-terminal Domain of the RNA Polymerase Alpha Subunit

Structural highlights

1z3e is a 2 chain structure with sequence from "bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	spxA ("Bacillus globigii" Migula 1900), rpoA ("Bacillus globigii" Migula 1900)
Activity:	DNA-directed RNA polymerase, with EC number 2.7.7.6
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SPX_BACSU] Interferes with activator-stimulated transcription by interaction with the RNA polymerase alpha-CTD. May function to globally reduce transcription of genes involved in growth- and development-promoting processes and to increase transcription of genes involved in thiol homeostasis, during periods of extreme stress. Negatively affects competence and sporulation. Its degradation by the MecA/ClpXP complex is needed for competence development.^[1] ^[2] [RPOA_BACSU] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Spx, a global transcription regulator in Bacillus subtilis, interacts with the C-terminal domain of the alpha subunit (alphaCTD) of RNA polymerase to control gene expression under conditions of disulfide stress, which is sensed by disulfide bond formation between Spx residues C10 and C13. Here, we describe the crystal structure of the B. subtilis alphaCTD bound to oxidized Spx. Analysis of the complex reveals interactions between three regions of "anti-alpha" Spx and helix alpha1 and the "261" determinant of alphaCTD. The former contact could disrupt the interaction between alphaCTD and activator proteins or alter the DNA-bound conformation of alphaCTD, thereby repressing activator-stimulated transcription. Binding to the 261 determinant would prevent interaction between alphaCTD and region 4 of sigma(A). Intriguingly, the Spx disulfide bond is far from the alphaCTD-Spx interface, suggesting that Spx regulates transcription allosterically or through the redox-dependent creation or destruction of binding sites for additional components of the transcription machinery.

Crystal structure of the Bacillus subtilis anti-alpha, global transcriptional regulator, Spx, in complex with the alpha C-terminal domain of RNA polymerase.,Newberry KJ, Nakano S, Zuber P, Brennan RG Proc Natl Acad Sci U S A. 2005 Nov 1;102(44):15839-44. Epub 2005 Oct 25. PMID:16249335^[3]

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

References

↑ Nakano MM, Hajarizadeh F, Zhu Y, Zuber P. Loss-of-function mutations in yjbD result in ClpX- and ClpP-independent competence development of Bacillus subtilis. Mol Microbiol. 2001 Oct;42(2):383-94. PMID:11703662
↑ Nakano S, Nakano MM, Zhang Y, Leelakriangsak M, Zuber P. A regulatory protein that interferes with activator-stimulated transcription in bacteria. Proc Natl Acad Sci U S A. 2003 Apr 1;100(7):4233-8. Epub 2003 Mar 17. PMID:12642660 doi:http://dx.doi.org/10.1073/pnas.0637648100
↑ Newberry KJ, Nakano S, Zuber P, Brennan RG. Crystal structure of the Bacillus subtilis anti-alpha, global transcriptional regulator, Spx, in complex with the alpha C-terminal domain of RNA polymerase. Proc Natl Acad Sci U S A. 2005 Nov 1;102(44):15839-44. Epub 2005 Oct 25. PMID:16249335

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1z3e"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Spx in Complex with the C-terminal Domain of the RNA Polymerase Alpha Subunit==
 <StructureSection load='1z3e' size='340' side='right' caption='[[1z3e]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spxA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900]), rpoA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</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=1z3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z3e OCA], [http://pdbe.org/1z3e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z3e RCSB], [http://www.ebi.ac.uk/pdbsum/1z3e PDBsum]</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=1z3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z3e OCA], [http://pdbe.org/1z3e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z3e RCSB], [http://www.ebi.ac.uk/pdbsum/1z3e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1z3e ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1z3e" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[RNA polymerase|RNA polymerase]]
 == References ==
 <references/>

1z3e

From Proteopedia

Revision as of 16:12, 12 October 2017

Crystal Structure of Spx in Complex with the C-terminal Domain of the RNA Polymerase Alpha Subunit

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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