2p4b
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='2p4b' size='340' side='right'caption='[[2p4b]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='2p4b' size='340' side='right'caption='[[2p4b]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2p4b]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2p4b]] is a 3 chain structure with sequence from [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=2P4B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P4B FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene></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=2p4b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p4b OCA], [https://pdbe.org/2p4b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p4b RCSB], [https://www.ebi.ac.uk/pdbsum/2p4b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p4b ProSAT]</span></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=2p4b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p4b OCA], [https://pdbe.org/2p4b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p4b RCSB], [https://www.ebi.ac.uk/pdbsum/2p4b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p4b ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/RSEB_ECOLI RSEB_ECOLI] Seems to modulate the activity of RpoE (sigma-E). | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 20: | Line 20: | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2p4b ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2p4b ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The bacterial envelope stress response senses stress signals in the extracytoplasmic compartment, and activates sigma(E)-dependent transcription by degrading its antisigma factor RseA. RseB, a binding partner of RseA, plays a pivotal role in regulating this response, but its molecular mechanism is not understood. We therefore determined the crystal structure of Escherichia coli RseB at a resolution of 2.4 A. RseB is composed of two domains linked by a flexible linker and forms a loosely packed dimer with two grooves on each side. This structural feature is confirmed by small-angle scattering in solution. Analysis of the binding of various RseA mutants to RseB allowed us to identify the major RseB-binding motif in RseA. These data, coupled with analysis of small-angle scattering of the RseA/RseB complex in solution, leads us to propose that two RseAs bind to the grooves of the dimeric RseB by conserved residues. The implications for modulating proteolytic cleavage of RseA are discussed. | ||
| - | |||
| - | Crystal structure of RseB and a model of its binding mode to RseA.,Kim DY, Jin KS, Kwon E, Ree M, Kim KK Proc Natl Acad Sci U S A. 2007 May 22;104(21):8779-84. Epub 2007 May 11. PMID:17496148<ref>PMID:17496148</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2p4b" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli K-12]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Kim | + | [[Category: Kim DY]] |
| - | [[Category: Kim | + | [[Category: Kim KK]] |
| - | + | ||
| - | + | ||
Current revision
Crystal structure of E.coli RseB
| |||||||||||
