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6a83

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Crystal structure of the C-terminal periplasmic domain of EcEptC from Escherichia coli complex with Zn

Structural highlights

6a83 is a 1 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.602Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

EPTC_ECOLI Catalyzes the addition of a phosphoethanolamine moiety to the outer membrane lipopolysaccharide core.

Publication Abstract from PubMed

Gram-negative bacteria defend against the toxicity of polymyxins by modifying their outer membrane lipopolysaccharide (LPS). This modification mainly occurs through the addition of cationic molecules such as phosphoethanolamine (PEA). EcEptC is a PEA transferase from Escherichia coli (E. coli). However, unlike its homologs CjEptC (Campylobacter jejuni) and MCR-1, EcEptC is unable to mediate polymyxin resistance when overexpressed in E. coli. Here, we report crystal structures of the C-terminal putative catalytic domain (EcEptCDeltaN, 205-577 aa) of EcEptC in apo and Zn(2+) -bound states at 2.10 and 2.60 A, respectively. EcEptCDeltaN is arranged into an alpha-beta-alpha fold and equipped with the zinc ion in a conserved mode. Coupled with isothermal titration calorimetry (ITC) data, we provide insights into the mechanism by which EcEptC recognizes Zn(2+) . Furthermore, structure comparison analysis indicated that disulfide bonds, which play a key role in polymyxin resistance, were absent in EcEptCDeltaN. Supported by structural and biochemical evidence, we reveal mechanistic implications for disulfide bonds in PEA transferase-mediated polymyxin resistance. Significantly, because the structural effects exhibited by disulfide bonds are absent in EcEptC, it is impossible for this protein to participate in polymyxin resistance in E. coli. DATABASE: Structural data are available in the PDB under the accession numbers 6A82 and 6A83. ENZYME: EC 2.7.8.43.

Structural and mechanistic insights into polymyxin resistance mediated by EptC originating from Escherichia coli.,Zhao Y, Meng Q, Lai Y, Wang L, Zhou D, Dou C, Gu Y, Nie C, Wei Y, Cheng W FEBS J. 2018 Dec 7. doi: 10.1111/febs.14719. PMID:30537137^[1]

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

References

↑ Zhao Y, Meng Q, Lai Y, Wang L, Zhou D, Dou C, Gu Y, Nie C, Wei Y, Cheng W. Structural and mechanistic insights into polymyxin resistance mediated by EptC originating from Escherichia coli. FEBS J. 2018 Dec 7. doi: 10.1111/febs.14719. PMID:30537137 doi:http://dx.doi.org/10.1111/febs.14719

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/6a83"

Categories: Escherichia coli K-12 | Large Structures | Cheng W | Gu YJ | Zhao YQ

@@ Line 1: / Line 1: @@
 ==Crystal structure of the C-terminal periplasmic domain of EcEptC from Escherichia coli complex with Zn==
-<StructureSection load='6a83' size='340' side='right'  caption='[[6a83]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+<StructureSection load='6a83' size='340' side='right'caption='[[6a83]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6a83]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A83 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A83 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6a83]] is a 1 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=6A83 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A83 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 2.602&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">eptC, cptA, yijP, b3955, JW3927 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=6a83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a83 OCA], [http://pdbe.org/6a83 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a83 RCSB], [http://www.ebi.ac.uk/pdbsum/6a83 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a83 ProSAT]</span></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=6a83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a83 OCA], [https://pdbe.org/6a83 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a83 RCSB], [https://www.ebi.ac.uk/pdbsum/6a83 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a83 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/EPTC_ECOLI EPTC_ECOLI]] Catalyzes the addition of a phosphoethanolamine moiety to the outer membrane lipopolysaccharide core.
+[https://www.uniprot.org/uniprot/EPTC_ECOLI EPTC_ECOLI] Catalyzes the addition of a phosphoethanolamine moiety to the outer membrane lipopolysaccharide core.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Ecoli]]
+[[Category: Escherichia coli K-12]]
-[[Category: Cheng, W]]
+[[Category: Large Structures]]
-[[Category: Gu, Y J]]
+[[Category: Cheng W]]
-[[Category: Zhao, Y Q]]
+[[Category: Gu YJ]]
-[[Category: Phosphoethanolamine transferase]]
+[[Category: Zhao YQ]]
-[[Category: Transferase]]

6a83

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Current revision

Crystal structure of the C-terminal periplasmic domain of EcEptC from Escherichia coli complex with Zn

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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