3n79

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Current revision (10:28, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3n79' size='340' side='right'caption='[[3n79]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='3n79' size='340' side='right'caption='[[3n79]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3n79]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N79 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3N79 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3n79]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N79 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N79 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pduT, STM2054 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<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=3n79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n79 OCA], [http://pdbe.org/3n79 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3n79 RCSB], [http://www.ebi.ac.uk/pdbsum/3n79 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3n79 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3n79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n79 OCA], [https://pdbe.org/3n79 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n79 RCSB], [https://www.ebi.ac.uk/pdbsum/3n79 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n79 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PDUT_SALTY PDUT_SALTY] A minor shell protein of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. The isolated BMC shell component protein ratio for J:A:B':B:K:T:U is approximately 15:10:7:6:1:1:2 (PubMed:12923081). Not required for structural integrity of BMCs nor to mitigate propionaldehyde toxicity, may selectively transport specific metabolites (PubMed:21239588). May be involved in electron transport across the BMC shell (Probable). Can be engineered to alter permeability of the BMC shell (PubMed:31674899).<ref>PMID:12923081</ref> <ref>PMID:21239588</ref> <ref>PMID:31674899</ref> <ref>PMID:20870711</ref> The 1,2-PD-specific bacterial microcompartment (BMC) concentrates low levels of 1,2-PD catabolic enzymes, concentrates volatile reaction intermediates thus enhancing pathway flux and keeps the level of toxic, mutagenic propionaldehyde low.<ref>PMID:28475631</ref>
== 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=3n79 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=3n79 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Bacterial microcompartments are a functionally diverse group of proteinaceous organelles that confine specific reaction pathways in the cell within a thin protein-based shell. The propanediol utilizing (Pdu) microcompartment contains the reactions for metabolizing 1,2-propanediol in certain enteric bacteria, including Salmonella. The Pdu shell is assembled from a few thousand protein subunits of several different types. Here we report the crystal structures of two key shell proteins, PduA and PduT. The crystal structures offer insights into the mechanisms of Pdu microcompartment assembly and molecular transport across the shell. PduA forms a symmetric homohexamer whose central pore appears tailored for facilitating transport of the 1,2-propanediol substrate. PduT is a novel, tandem domain shell protein that assembles as a pseudohexameric homotrimer. Its structure reveals an unexpected site for binding an [Fe-S] cluster at the center of the PduT pore. The location of a metal redox cofactor in the pore of a shell protein suggests a novel mechanism for either transferring redox equivalents across the shell or for regenerating luminal [Fe-S] clusters.
 
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Structural insights into the mechanisms of transport across the Salmonella enterica Pdu microcompartment shell.,Crowley CS, Cascio D, Sawaya MR, Kopstein JS, Bobik TA, Yeates TO J Biol Chem. 2010 Sep 24. PMID:20870711<ref>PMID:20870711</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 3n79" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus typhimurium loeffler 1892]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cascio, D]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
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[[Category: Crowley, C S]]
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[[Category: Cascio D]]
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[[Category: Sawaya, M R]]
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[[Category: Crowley CS]]
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[[Category: Yeates, T O]]
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[[Category: Sawaya MR]]
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[[Category: Bmc shell protein]]
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[[Category: Yeates TO]]
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[[Category: Carboxysome]]
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[[Category: Electron transport]]
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[[Category: Fes cluster]]
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[[Category: Pdu]]
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Current revision

PduT C38S Mutant from Salmonella enterica Typhimurium

PDB ID 3n79

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