4lqe: Difference between revisions

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{{STRUCTURE_4lqe|  PDB=4lqe  |  SCENE=  }}
===Crystal Structure of MepB===
{{ABSTRACT_PUBMED_24501097}}


==About this Structure==
==Crystal Structure of MepB==
[[4lqe]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LQE OCA].  
<StructureSection load='4lqe' size='340' side='right'caption='[[4lqe]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4lqe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_Mu50 Staphylococcus aureus subsp. aureus Mu50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LQE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LQE 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]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4lqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lqe OCA], [https://pdbe.org/4lqe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lqe RCSB], [https://www.ebi.ac.uk/pdbsum/4lqe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lqe ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The MepRAB operon in Staphylococcus aureus has been identified to play a role in drug resistance. Although the functions of MepA and MepR are known, little information is available on the function of MepB. Here we report the X-ray structure of MepB to 2.1 A revealing its structural similarity to the PD-(D/E)XK family of endonucleases. We further show that MepB binds DNA and RNA, with a higher affinity towards RNA and single stranded DNA than towards double stranded DNA. Notably, the PD-(D/E)XK catalytic active site residues are not conserved in MepB. MepB's association with a drug resistance operon suggests that it plays a role in responding to antimicrobials. This role is likely carried out through MepB's interactions with nucleic acids.


==Reference==
Structural characterization of MepB from Staphylococcus aureus reveals homology to endonucleases.,Agah S, Poulos S, Banchs C, Faham S Protein Sci. 2014 Feb 6. doi: 10.1002/pro.2438. PMID:24501097<ref>PMID:24501097</ref>
<ref group="xtra">PMID:024501097</ref><references group="xtra"/><references/>
 
[[Category: Agah, S.]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Faham, S.]]
</div>
[[Category: Dna binding protein]]
<div class="pdbe-citations 4lqe" style="background-color:#fffaf0;"></div>
[[Category: Endonuclease]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus subsp. aureus Mu50]]
[[Category: Agah S]]
[[Category: Faham S]]
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