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| | <StructureSection load='6od1' size='340' side='right'caption='[[6od1]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='6od1' size='340' side='right'caption='[[6od1]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6od1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OD1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OD1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6od1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_907672 Escherichia coli 907672] and [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OD1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OD1 FirstGlance]. <br> |
| - | </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=6od1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6od1 OCA], [http://pdbe.org/6od1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6od1 RCSB], [http://www.ebi.ac.uk/pdbsum/6od1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6od1 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]] 2Å</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=6od1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6od1 OCA], [https://pdbe.org/6od1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6od1 RCSB], [https://www.ebi.ac.uk/pdbsum/6od1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6od1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/V0SNG0_ECOLX V0SNG0_ECOLX]] Regulates the turnover of the sigma S factor (RpoS) by promoting its proteolysis in exponentially growing cells. Acts by binding and delivering RpoS to the ClpXP protease. RssB is not co-degraded with RpoS, but is released from the complex and can initiate a new cycle of RpoS recognition and degradation.[HAMAP-Rule:MF_00958] [[http://www.uniprot.org/uniprot/IRAD_ECOLI IRAD_ECOLI]] Inhibits RpoS proteolysis by regulating RssB activity, thereby increasing the stability of the sigma stress factor RpoS during oxidative stress. Its effect on RpoS stability is due to its interaction with RssB, which probably blocks the interaction of RssB with RpoS, and the consequent delivery of the RssB-RpoS complex to the ClpXP protein degradation pathway.<ref>PMID:18383615</ref> | + | [https://www.uniprot.org/uniprot/V0SNG0_ECOLX V0SNG0_ECOLX] Regulates the turnover of the sigma S factor (RpoS) by promoting its proteolysis in exponentially growing cells. Acts by binding and delivering RpoS to the ClpXP protease. RssB is not co-degraded with RpoS, but is released from the complex and can initiate a new cycle of RpoS recognition and degradation.[HAMAP-Rule:MF_00958] |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | The stationary phase promoter specificity subunit sigma(S) (RpoS) is delivered to the ClpXP machinery for degradation dependent on the adaptor RssB. This adaptor-specific degradation of sigma(S) provides a major point for regulation and transcriptional reprogramming during the general stress response. RssB is an atypical response regulator and the only known ClpXP adaptor that is inhibited by multiple but dissimilar antiadaptors (IraD, IraP, and IraM). These are induced by distinct stress signals and bind to RssB in poorly understood manners to achieve stress-specific inhibition of sigma(S) turnover. Here we present the first crystal structure of RssB bound to an antiadaptor, the DNA damage-inducible IraD. The structure reveals that RssB adopts a compact closed architecture with extensive interactions between its N-terminal and C-terminal domains. The structural data, together with mechanistic studies, suggest that RssB plasticity, conferred by an interdomain glutamate-rich flexible linker, is critical for regulation of sigma(S) degradation. Structural modulation of interdomain linkers may thus constitute a general strategy for tuning response regulators.
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| - | Structural basis for inhibition of a response regulator of sigma(S) stability by a ClpXP antiadaptor.,Dorich V, Brugger C, Tripathi A, Hoskins JR, Tong S, Suhanovsky MM, Sastry A, Wickner S, Gottesman S, Deaconescu AM Genes Dev. 2019 Apr 11. pii: gad.320168.118. doi: 10.1101/gad.320168.118. PMID:30975721<ref>PMID:30975721</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 6od1" style="background-color:#fffaf0;"></div>
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| - | == References ==
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| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Escherichia coli 907672]] |
| | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Deaconescu, A M]] | + | [[Category: Deaconescu AM]] |
| - | [[Category: Dorich, V]] | + | [[Category: Dorich V]] |
| - | [[Category: Anti-adaptor]]
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| - | [[Category: Clpxp adaptor]]
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| - | [[Category: Dna damage]]
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| - | [[Category: Gp25]]
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| - | [[Category: Response regulator]]
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| - | [[Category: Signaling protein]]
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