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5njb

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'''Unreleased structure'''
 
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The entry 5njb is ON HOLD until Paper Publication
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==E. coli Microcin-processing metalloprotease TldD/E with actinonin bound==
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<StructureSection load='5njb' size='340' side='right'caption='[[5njb]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5njb]] is a 4 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=5NJB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NJB FirstGlance]. <br>
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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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BB2:ACTINONIN'>BB2</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5njb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5njb OCA], [https://pdbe.org/5njb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5njb RCSB], [https://www.ebi.ac.uk/pdbsum/5njb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5njb ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TLDD_ECOLI TLDD_ECOLI] Metalloprotease involved in CcdA degradation. Suppresses the inhibitory activity of the carbon storage regulator (CsrA).<ref>PMID:12029038</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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TldD and TldE proteins are involved in the biosynthesis of microcin B17 (MccB17), an Escherichia coli thiazole/oxazole-modified peptide toxin targeting DNA gyrase. Using a combination of biochemical and crystallographic methods we show that E. coli TldD and TldE interact to form a heterodimeric metalloprotease. TldD/E cleaves the N-terminal leader sequence from the modified MccB17 precursor peptide, to yield mature antibiotic, while it has no effect on the unmodified peptide. Both proteins are essential for the activity; however, only the TldD subunit forms a novel metal-containing active site within the hollow core of the heterodimer. Peptide substrates are bound in a sequence-independent manner through beta sheet interactions with TldD and are likely cleaved via a thermolysin-type mechanism. We suggest that TldD/E acts as a "molecular pencil sharpener": unfolded polypeptides are fed through a narrow channel into the active site and processively truncated through the cleavage of short peptides from the N-terminal end.
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Authors:
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The Origins of Specificity in the Microcin-Processing Protease TldD/E.,Ghilarov D, Serebryakova M, Stevenson CEM, Hearnshaw SJ, Volkov D, Maxwell A, Lawson DM, Severinov K Structure. 2017 Sep 11. pii: S0969-2126(17)30259-9. doi:, 10.1016/j.str.2017.08.006. PMID:28943336<ref>PMID:28943336</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5njb" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli K-12]]
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[[Category: Large Structures]]
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[[Category: Ghilarov D]]
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[[Category: Hearnshaw SJ]]
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[[Category: Lawson DM]]
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[[Category: Maxwell A]]
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[[Category: Serebryakova M]]
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[[Category: Severinov K]]
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[[Category: Stevenson CEM]]
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[[Category: Volkov D]]

Current revision

E. coli Microcin-processing metalloprotease TldD/E with actinonin bound

PDB ID 5njb

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