5nja: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 5nja is ~~ON HOLD~~ ~~until Paper~~ Publication

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

== 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NJA 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=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'>[http://oca.weizmann.ac.il/oca-docs/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>

</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>

== 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.

~~Authors~~:

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>

~~Description~~:

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

[[Category: ~~Unreleased Structures~~]]

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Ghilarov, D]]

[[Category: Hearnshaw, S J]]

[[Category: Lawson, D M]]

[[Category: Maxwell, A]]

[[Category: Serebryakova, M]]

[[Category: Severinov, K]]

[[Category: Stevenson, C E.M]]

[[Category: Volkov, D]]

[[Category: Ccda]]

[[Category: Dna gyrase]]

[[Category: Hydrolase]]

[[Category: Metalloprotease]]

[[Category: Microcin]]

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5nja is ON HOLD  until Paper Publication
+==E. coli Microcin-processing metalloprotease TldD/E with angiotensin analogue bound==
+<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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NJA 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=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'>[http://oca.weizmann.ac.il/oca-docs/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>
+</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>
+<div style="background-color:#fffaf0;">
+== 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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5nja" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Ghilarov, D]]
+[[Category: Hearnshaw, S J]]
+[[Category: Lawson, D M]]
+[[Category: Maxwell, A]]
+[[Category: Serebryakova, M]]
+[[Category: Severinov, K]]
+[[Category: Stevenson, C E.M]]
+[[Category: Volkov, D]]
+[[Category: Ccda]]
+[[Category: Dna gyrase]]
+[[Category: Hydrolase]]
+[[Category: Metalloprotease]]
+[[Category: Microcin]]