6g4h

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<StructureSection load='6g4h' size='340' side='right'caption='[[6g4h]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='6g4h' size='340' side='right'caption='[[6g4h]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6g4h]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G4H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6G4H FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6g4h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G4H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6G4H 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=EMC:ETHYL+MERCURY+ION'>EMC</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6g49|6g49]]</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=EMC:ETHYL+MERCURY+ION'>EMC</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-glutamine_gamma-glutamyltransferase Protein-glutamine gamma-glutamyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.13 2.3.2.13] </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=6g4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g4h OCA], [https://pdbe.org/6g4h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6g4h RCSB], [https://www.ebi.ac.uk/pdbsum/6g4h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6g4h ProSAT]</span></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=6g4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g4h OCA], [http://pdbe.org/6g4h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6g4h RCSB], [http://www.ebi.ac.uk/pdbsum/6g4h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6g4h ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/TGPA_PSEAE TGPA_PSEAE]] Displays transglutaminase activity (TGase) in vitro. Plays a critical role in the viability of P.aeruginosa. Might contribute to an essential function linked to the cell wall.<ref>PMID:23209712</ref>
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[https://www.uniprot.org/uniprot/TGPA_PSEAE TGPA_PSEAE] Displays transglutaminase activity (TGase) in vitro. Plays a critical role in the viability of P.aeruginosa. Might contribute to an essential function linked to the cell wall.<ref>PMID:23209712</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Pseudomonas aeruginosa is an opportunistic pathogen associated with severe diseases, such as cystic fibrosis. During an extensive search for novel essential genes, we identified tgpA (locus PA2873) in P. aeruginosa PAO1, as a gene playing a critical role in bacterial viability. TgpA, the translated protein, is an internal membrane protein with a periplasmic soluble domain, predicted to be endowed with a transglutaminase-like fold, hosting the Cys404, His448, and Asp464 triad. We report here that Cys404 mutation hampers the essential role of TgpA in granting P. aeruginosa viability. Moreover, we present the crystal structure of the TgpA periplasmic domain at 1.6A resolution as a first step towards structure-activity analysis of a new potential target for the discovery of antibacterial compounds.
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Structural and functional characterization of TgpA, a critical protein for the viability of Pseudomonas aeruginosa.,Uruburu M, Mastrangelo E, Bolognesi M, Ferrara S, Bertoni G, Milani M J Struct Biol. 2019 Mar 1;205(3):18-25. doi: 10.1016/j.jsb.2018.12.004. Epub 2018, Dec 30. PMID:30599211<ref>PMID:30599211</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 6g4h" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Protein-glutamine gamma-glutamyltransferase]]
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[[Category: Pseudomonas aeruginosa PAO1]]
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[[Category: Mastrangelo, E]]
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[[Category: Mastrangelo E]]
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[[Category: Milani, M]]
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[[Category: Milani M]]
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[[Category: Uruburu, M]]
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[[Category: Uruburu M]]
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[[Category: Essential bacterial protein]]
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[[Category: Transferase]]
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Current revision

Crystal structure of the periplasmic domain of TgpA from Pseudomonas aeruginosa bound to ethylmercury

PDB ID 6g4h

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