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| <StructureSection load='3sg9' size='340' side='right'caption='[[3sg9]], [[Resolution|resolution]] 2.15Å' scene=''> | | <StructureSection load='3sg9' size='340' side='right'caption='[[3sg9]], [[Resolution|resolution]] 2.15Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3sg9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"streptococcus_casseliflavus"_vaughan_et_al._1979 "streptococcus casseliflavus" vaughan et al. 1979]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SG9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SG9 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3sg9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_casseliflavus Enterococcus casseliflavus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SG9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SG9 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=KAN:KANAMYCIN+A'>KAN</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]] 2.15Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aph(2'')-Id ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=37734 "Streptococcus casseliflavus" Vaughan et al. 1979])</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=KAN:KANAMYCIN+A'>KAN</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=3sg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sg9 OCA], [https://pdbe.org/3sg9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sg9 RCSB], [https://www.ebi.ac.uk/pdbsum/3sg9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sg9 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=3sg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sg9 OCA], [https://pdbe.org/3sg9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sg9 RCSB], [https://www.ebi.ac.uk/pdbsum/3sg9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sg9 ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/O68183_ENTCA O68183_ENTCA] |
| Aminoglycoside 2''-phosphotransferase IVa [APH(2'')-IVa] is a member of a family of bacterial enzymes responsible for medically relevant resistance to antibiotics. APH(2'')-IVa confers high-level resistance against several clinically used aminoglycoside antibiotics in various pathogenic Enterococcus species by phosphorylating the drug, thereby preventing it from binding to its ribosomal target and producing a bactericidal effect. We describe here three crystal structures of APH(2'')-IVa, one in its apo form and two in complex with a bound antibiotic, tobramycin and kanamycin A. The apo structure was refined to a resolution of 2.05 A, and the APH(2'')-IVa structures with tobramycin and kanamycin A bound were refined to resolutions of 1.80 and 2.15 A, respectively. Comparison among the structures provides insight concerning the substrate selectivity of this enzyme. In particular, conformational changes upon substrate binding, involving rotational shifts of two distinct segments of the enzyme, are observed. These substrate-induced shifts may also rationalize the altered substrate preference of APH(2'')-IVa in comparison to those of other members of the APH(2'') subfamily, which are structurally closely related. Finally, analysis of the interactions between the enzyme and aminoglycoside reveals a distinct binding mode as compared to the intended ribosomal target. The differences in the pattern of interactions can be utilized as a structural basis for the development of improved aminoglycosides that are not susceptible to these resistance factors.
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| Crystal Structures of Antibiotic-Bound Complexes of Aminoglycoside 2''-Phosphotransferase IVa Highlight the Diversity in Substrate Binding Modes among Aminoglycoside Kinases.,Shi K, Houston DR, Berghuis AM Biochemistry. 2011 Jun 27. PMID:21678960<ref>PMID:21678960</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 3sg9" 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]] |
| == References ==
| |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Streptococcus casseliflavus vaughan et al. 1979]] | | [[Category: Enterococcus casseliflavus]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Berghuis, A M]] | | [[Category: Berghuis AM]] |
| [[Category: Houston, D R]] | | [[Category: Houston DR]] |
| [[Category: Shi, K]] | | [[Category: Shi K]] |
| [[Category: Aminoglycoside]]
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| [[Category: Antibiotic resistance enzyme]]
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| [[Category: Phosphotransferase]]
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| [[Category: Transferase]]
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| [[Category: Transferase-antibiotic complex]]
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