1oul: Difference between revisions

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<StructureSection load='1oul' size='340' side='right'caption='[[1oul]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='1oul' size='340' side='right'caption='[[1oul]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1oul]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OUL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1OUL FirstGlance]. <br>
<table><tr><td colspan='2'>[[1oul]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OUL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OUL FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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]] 2.2&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ou8|1ou8]], [[1ou9|1ou9]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SSPB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 "Bacterium influenzae" Lehmann and Neumann 1896])</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=1oul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oul OCA], [https://pdbe.org/1oul PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oul RCSB], [https://www.ebi.ac.uk/pdbsum/1oul PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oul 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=1oul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oul OCA], [http://pdbe.org/1oul PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oul RCSB], [http://www.ebi.ac.uk/pdbsum/1oul PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1oul ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SSPB_HAEIN SSPB_HAEIN]] Enhances recognition of ssrA-tagged proteins by the ClpX-ClpP protease; the ssrA degradation tag (AANDENYALAA) is added trans-translationally to proteins that are stalled on the ribosome, freeing the ribosome and targeting stalled peptides for degradation. SspB activates the ATPase activity of ClpX. Seems to act in concert with SspA in the regulation of several proteins during exponential and stationary-phase growth (By similarity).  Also stimulates degradation of the N-terminus of RseA (residues 1-108, alone or in complex with sigma-E) by ClpX-ClpP in a non-ssrA-mediated fashion (By similarity).  
[https://www.uniprot.org/uniprot/SSPB_HAEIN SSPB_HAEIN] Enhances recognition of ssrA-tagged proteins by the ClpX-ClpP protease; the ssrA degradation tag (AANDENYALAA) is added trans-translationally to proteins that are stalled on the ribosome, freeing the ribosome and targeting stalled peptides for degradation. SspB activates the ATPase activity of ClpX. Seems to act in concert with SspA in the regulation of several proteins during exponential and stationary-phase growth (By similarity).  Also stimulates degradation of the N-terminus of RseA (residues 1-108, alone or in complex with sigma-E) by ClpX-ClpP in a non-ssrA-mediated fashion (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1oul 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=1oul ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Substrate selection by AAA+ ATPases that function to unfold proteins or alter protein conformation is often regulated by delivery or adaptor proteins. SspB is a protein dimer that binds to the ssrA degradation tag and delivers proteins bearing this tag to ClpXP, an AAA+ protease, for degradation. Here, we describe the structure of the peptide binding domain of H. influenzae SspB in complex with an ssrA peptide at 1.6 A resolution. The ssrA peptides are bound in well-defined clefts located at the extreme ends of the SspB homodimer. SspB contacts residues within the N-terminal and central regions of the 11 residue ssrA tag but leaves the C-terminal residues exposed and positioned to dock with ClpX. This structure, taken together with biochemical analysis of SspB, suggests mechanisms by which proteins like SspB escort substrates to AAA+ ATPases and enhance the specificity and affinity of target recognition.


Structure of a delivery protein for an AAA+ protease in complex with a peptide degradation tag.,Levchenko I, Grant RA, Wah DA, Sauer RT, Baker TA Mol Cell. 2003 Aug;12(2):365-72. PMID:14536076<ref>PMID:14536076</ref>
==See Also==
 
*[[Stringent starvation protein 3D structures|Stringent starvation protein 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1oul" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacterium influenzae lehmann and neumann 1896]]
[[Category: Haemophilus influenzae]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Baker, T A]]
[[Category: Baker TA]]
[[Category: Grant, R A]]
[[Category: Grant RA]]
[[Category: Levchenko, I]]
[[Category: Levchenko I]]
[[Category: Sauer, R T]]
[[Category: Sauer RT]]
[[Category: Wah, D A]]
[[Category: Wah DA]]
[[Category: Homodimer]]
[[Category: Ssra peptide binding protein]]
[[Category: Transport protein]]
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