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5ih1

From Proteopedia

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<StructureSection load='5ih1' size='340' side='right'caption='[[5ih1]], [[Resolution|resolution]] 1.31&Aring;' scene=''>
<StructureSection load='5ih1' size='340' side='right'caption='[[5ih1]], [[Resolution|resolution]] 1.31&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5ih1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IH1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IH1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5ih1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IH1 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6BQ:PHOSPHORYLATED+JOSAMYCIN'>6BQ</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.31&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5igu|5igu]], [[5igv|5igv]], [[5igw|5igw]], [[5igy|5igy]], [[5igz|5igz]], [[5ih0|5ih0]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6BQ:PHOSPHORYLATED+JOSAMYCIN'>6BQ</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mphB, pO103_99 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ih1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ih1 OCA], [https://pdbe.org/5ih1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ih1 RCSB], [https://www.ebi.ac.uk/pdbsum/5ih1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ih1 ProSAT]</span></td></tr>
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<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=5ih1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ih1 OCA], [http://pdbe.org/5ih1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ih1 RCSB], [http://www.ebi.ac.uk/pdbsum/5ih1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ih1 ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/O32553_ECOLX O32553_ECOLX]
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5ih1" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Phosphotransferase 3D structures|Phosphotransferase 3D structures]]
*[[Phosphotransferase 3D structures|Phosphotransferase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus coli migula 1895]]
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[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Berghuis, A M]]
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[[Category: Berghuis AM]]
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[[Category: Fong, D H]]
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[[Category: Fong DH]]
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[[Category: Kinase]]
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[[Category: Macrolide phosphotransferase]]
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[[Category: Transferase]]
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Current revision

Macrolide 2'-phosphotransferase type II - complex with GDP and phosphorylated josamycin

PDB ID 5ih1

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