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5nja

From Proteopedia

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E. coli Microcin-processing metalloprotease TldD/E with angiotensin analogue bound

Structural highlights

5nja is a 6 chain structure with sequence from Escherichia coli str. K-12 substr. MG1655 and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.4Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TLDD_ECOLI Metalloprotease involved in CcdA degradation. Suppresses the inhibitory activity of the carbon storage regulator (CsrA).^[1]

Publication Abstract from PubMed

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Allali N, Afif H, Couturier M, Van Melderen L. The highly conserved TldD and TldE proteins of Escherichia coli are involved in microcin B17 processing and in CcdA degradation. J Bacteriol. 2002 Jun;184(12):3224-31. PMID:12029038
↑ Ghilarov D, Serebryakova M, Stevenson CEM, Hearnshaw SJ, Volkov D, Maxwell A, Lawson DM, Severinov K. The Origins of Specificity in the Microcin-Processing Protease TldD/E. Structure. 2017 Sep 11. pii: S0969-2126(17)30259-9. doi:, 10.1016/j.str.2017.08.006. PMID:28943336 doi:http://dx.doi.org/10.1016/j.str.2017.08.006

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5nja"

@@ Line 3: / Line 3: @@
 <StructureSection load='5nja' size='340' side='right'caption='[[5nja]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5nja]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NJA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5NJA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5nja]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._MG1655 Escherichia coli str. K-12 substr. MG1655] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NJA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NJA FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.4&#8491;</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=5nja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nja OCA], [http://pdbe.org/5nja PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nja RCSB], [http://www.ebi.ac.uk/pdbsum/5nja PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nja ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5nja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nja OCA], [https://pdbe.org/5nja PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nja RCSB], [https://www.ebi.ac.uk/pdbsum/5nja PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nja ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>  [[http://www.uniprot.org/uniprot/PMBA_ECOLI PMBA_ECOLI]] Metalloprotease involved in CcdA degradation. Suppresses the inhibitory activity of the carbon storage regulator (CsrA).<ref>PMID:12029038</ref>
+[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
+[[Category: Escherichia coli str. K-12 substr. MG1655]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Ghilarov, D]]
+[[Category: Ghilarov D]]
-[[Category: Hearnshaw, S J]]
+[[Category: Hearnshaw SJ]]
-[[Category: Lawson, D M]]
+[[Category: Lawson DM]]
-[[Category: Maxwell, A]]
+[[Category: Maxwell A]]
-[[Category: Serebryakova, M]]
+[[Category: Serebryakova M]]
-[[Category: Severinov, K]]
+[[Category: Severinov K]]
-[[Category: Stevenson, C E.M]]
+[[Category: Stevenson CEM]]
-[[Category: Volkov, D]]
+[[Category: Volkov D]]
-[[Category: Ccda]]
-[[Category: Dna gyrase]]
-[[Category: Hydrolase]]
-[[Category: Metalloprotease]]
-[[Category: Microcin]]

5nja

From Proteopedia

Current revision

E. coli Microcin-processing metalloprotease TldD/E with angiotensin analogue bound

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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