6xcs: Difference between revisions

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<StructureSection load='6xcs' size='340' side='right'caption='[[6xcs]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='6xcs' size='340' side='right'caption='[[6xcs]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6xcs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XCS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XCS FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XCS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XCS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</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]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=6xcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xcs OCA], [https://pdbe.org/6xcs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xcs RCSB], [https://www.ebi.ac.uk/pdbsum/6xcs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xcs 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=6xcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xcs OCA], [https://pdbe.org/6xcs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xcs RCSB], [https://www.ebi.ac.uk/pdbsum/6xcs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xcs ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C7C425_KLEPN C7C425_KLEPN]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Macrolides are a class of antibiotics widely used in both medicine and agriculture. Unsurprisingly, as a consequence of their exensive usage a plethora of resistance mechanisms have been encountered in pathogenic bacteria. One of these resistance mechanisms entails the enzymatic cleavage of the macrolides' macrolactone ring by erythromycin esterases (Eres). The most frequently identified Ere enzyme is EreA, which confers resistance to the majority of clinically used macrolides. Despite the role Eres play in macrolide resistance, research into this family enzymes has been sparse. Here, we report the first three-dimensional structures of an erythromycin esterase, EreC. EreC is an extremely close homologue of EreA, displaying more than 90% sequence identity. Two structures of this enzyme, in conjunction with in silico flexible docking studies and previously reported mutagenesis data allowed for the proposal of a detailed catalytic mechanism for the Ere family of enzymes, labeling them as metal-independent hydrolases. Also presented are substrate spectrum assays for different members of the Ere family. The results from these assays together with an examination of residue conservation for the macrolide binding site in Eres, suggests two distinct active site archetypes within the Ere enzyme family.
Structural and functional insights into esterase-mediated macrolide resistance.,Zielinski M, Park J, Sleno B, Berghuis AM Nat Commun. 2021 Mar 19;12(1):1732. doi: 10.1038/s41467-021-22016-3. PMID:33741980<ref>PMID:33741980</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6xcs" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Klebsiella pneumoniae]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Berghuis AM]]
[[Category: Berghuis AM]]
[[Category: Zielinski M]]
[[Category: Zielinski M]]

Latest revision as of 14:23, 30 October 2024

Erythromycin esterase mutant EreC H289N in its open conformationErythromycin esterase mutant EreC H289N in its open conformation

Structural highlights

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

6xcs, resolution 2.40Å

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OCA
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