This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

5nj5

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

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

Structural highlights

5nj5 is a 4 chain structure with sequence from Escherichia coli str. K-12 substr. MG1655. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
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/5nj5"

@@ Line 1: / Line 1: @@
 ==E. coli Microcin-processing metalloprotease TldD/E with phosphate bound==
-<StructureSection load='5nj5' size='340' side='right' caption='[[5nj5]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+<StructureSection load='5nj5' size='340' side='right'caption='[[5nj5]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5nj5]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NJ5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NJ5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5nj5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._MG1655 Escherichia coli str. K-12 substr. MG1655]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NJ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NJ5 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.9&#8491;</td></tr>
-<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=5nj5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nj5 OCA], [http://pdbe.org/5nj5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nj5 RCSB], [http://www.ebi.ac.uk/pdbsum/5nj5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nj5 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=PO4:PHOSPHATE+ION'>PO4</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=5nj5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nj5 OCA], [https://pdbe.org/5nj5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nj5 RCSB], [https://www.ebi.ac.uk/pdbsum/5nj5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nj5 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: Ghilarov, D]]
+[[Category: Escherichia coli str. K-12 substr. MG1655]]
-[[Category: Hearnshaw, S J]]
+[[Category: Large Structures]]
-[[Category: Lawson, D M]]
+[[Category: Ghilarov D]]
-[[Category: Maxwell, A]]
+[[Category: Hearnshaw SJ]]
-[[Category: Serebryakova, M]]
+[[Category: Lawson DM]]
-[[Category: Severinov, K]]
+[[Category: Maxwell A]]
-[[Category: Stevenson, C E.M]]
+[[Category: Serebryakova M]]
-[[Category: Volkov, D]]
+[[Category: Severinov K]]
-[[Category: Ccda]]
+[[Category: Stevenson CEM]]
-[[Category: Dna gyrase]]
+[[Category: Volkov D]]
-[[Category: Hydrolase]]
-[[Category: Metalloprotease]]
-[[Category: Microcin]]

5nj5

From Proteopedia

Current revision

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

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox