View source for 5igp


==Macrolide 2'-phosphotransferase type I - complex with GDP and erythromycin==
<StructureSection load='5igp' size='340' side='right' caption='[[5igp]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5igp]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IGP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IGP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ERY:ERYTHROMYCIN+A'>ERY</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5igh|5igh]], [[5igi|5igi]], [[5igj|5igj]], [[5igr|5igr]], [[5igs|5igs]], [[5igt|5igt]], [[5igu|5igu]], [[5igv|5igv]], [[5igw|5igw]], [[5igy|5igy]], [[5igz|5igz]], [[5ih0|5ih0]], [[5ih1|5ih1]]</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=5igp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5igp OCA], [http://pdbe.org/5igp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5igp RCSB], [http://www.ebi.ac.uk/pdbsum/5igp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5igp ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The macrolides are a class of antibiotic, characterized by a large macrocyclic lactone ring that can be inactivated by macrolide phosphotransferase enzymes. We present structures for MPH(2')-I and MPH(2')-II in the apo state, and in complex with GTP analogs and six different macrolides. These represent the first structures from the two main classes of macrolide phosphotransferases. The structures show that the enzymes are related to the aminoglycoside phosphotransferases, but are distinguished from them by the presence of a large interdomain linker that contributes to an expanded antibiotic binding pocket. This pocket is largely hydrophobic, with a negatively charged patch located at a conserved aspartate residue, rationalizing the broad-spectrum resistance conferred by the enzymes. Complementary mutation studies provide insights into factors governing substrate specificity. A comparison with macrolides bound to their natural target, the 50S ribosome, suggests avenues for next-generation antibiotic development.

Structural Basis for Kinase-Mediated Macrolide Antibiotic Resistance.,Fong DH, Burk DL, Blanchet J, Yan AY, Berghuis AM Structure. 2017 May 2;25(5):750-761.e5. doi: 10.1016/j.str.2017.03.007. Epub 2017, Apr 13. PMID:28416110<ref>PMID:28416110</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5igp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Berghuis, A M]]
[[Category: Fong, D H]]
[[Category: Kinase]]
[[Category: Macrolide phosphotransferase]]
[[Category: Transferase-antibiotic complex]]