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| | ==Crystal structure of aminoglycoside-3'-phosphotransferase of type VIII== | | ==Crystal structure of aminoglycoside-3'-phosphotransferase of type VIII== |
| - | <StructureSection load='4h05' size='340' side='right' caption='[[4h05]], [[Resolution|resolution]] 2.15Å' scene=''> | + | <StructureSection load='4h05' size='340' side='right'caption='[[4h05]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4h05]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/As_4.1438 As 4.1438]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H05 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4H05 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4h05]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_rimosus Streptomyces rimosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H05 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H05 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AAG11411 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1927 AS 4.1438])</td></tr> | + | </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=4h05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h05 OCA], [https://pdbe.org/4h05 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h05 RCSB], [https://www.ebi.ac.uk/pdbsum/4h05 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h05 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Kanamycin_kinase Kanamycin kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.95 2.7.1.95] </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=4h05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h05 OCA], [http://pdbe.org/4h05 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4h05 RCSB], [http://www.ebi.ac.uk/pdbsum/4h05 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4h05 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9F9M5_STRRM Q9F9M5_STRRM] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Phosphotransferase|Phosphotransferase]] | + | *[[Phosphotransferase 3D structures|Phosphotransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: As 4 1438]] | + | [[Category: Large Structures]] |
| - | [[Category: Kanamycin kinase]] | + | [[Category: Streptomyces rimosus]] |
| - | [[Category: Alekseeva, M G]] | + | [[Category: Alekseeva MG]] |
| - | [[Category: Boyko, K M]] | + | [[Category: Boyko KM]] |
| - | [[Category: Danilenko, V N]] | + | [[Category: Danilenko VN]] |
| - | [[Category: Dorovatovskiy, P V]] | + | [[Category: Dorovatovskiy PV]] |
| - | [[Category: Gorbacheva, M A]] | + | [[Category: Gorbacheva MA]] |
| - | [[Category: Korzhenevskiy, D A]] | + | [[Category: Korzhenevskiy DA]] |
| - | [[Category: Lipkin, A V]] | + | [[Category: Lipkin AV]] |
| - | [[Category: Popov, V O]] | + | [[Category: Popov VO]] |
| - | [[Category: Aminoglycoside antibiotic]]
| + | |
| - | [[Category: Aminoglycoside phosphotransferase viii]]
| + | |
| - | [[Category: Atp binding]]
| + | |
| - | [[Category: Phosphorilation]]
| + | |
| - | [[Category: Protein kinase]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
Q9F9M5_STRRM
Publication Abstract from PubMed
Aminoglycoside phosphotransferases represent a broad class of enzymes that promote bacterial resistance to aminoglycoside antibiotics via the phosphorylation of hydroxyl groups in the latter. Here we report the spatial structure of the 3'-aminoglycoside phosphotransferase of novel VIII class (AphVIII) solved by X-ray diffraction method with a resolution of 2.15 A. Deep analysis of APHVIII structure and its comparison with known structures of aminoglycoside phosphotransferases of various types reveals that AphVIII has a typical two-domain fold and, however, possesses some unique characteristics that distinguish the enzyme from its known homologues. The most important difference is the presence of the activation loop with unique Ser146 residue. We demonstrate that in the apo-state of the enzyme the activation loop does not interact with other parts of the enzyme and seems to adopt catalytically competent state only after substrate binding.
Structural characterization of the novel aminoglycoside phosphotransferase AphVIII from Streptomyces rimosus with enzymatic activity modulated by phosphorylation.,Boyko KM, Gorbacheva MA, Korzhenevskiy DA, Alekseeva MG, Mavletova DA, Zakharevich NV, Elizarov SM, Rudakova NN, Danilenko VN, Popov VO Biochem Biophys Res Commun. 2016 Sep 2;477(4):595-601. doi:, 10.1016/j.bbrc.2016.06.097. Epub 2016 Jun 20. PMID:27338640[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Boyko KM, Gorbacheva MA, Korzhenevskiy DA, Alekseeva MG, Mavletova DA, Zakharevich NV, Elizarov SM, Rudakova NN, Danilenko VN, Popov VO. Structural characterization of the novel aminoglycoside phosphotransferase AphVIII from Streptomyces rimosus with enzymatic activity modulated by phosphorylation. Biochem Biophys Res Commun. 2016 Sep 2;477(4):595-601. doi:, 10.1016/j.bbrc.2016.06.097. Epub 2016 Jun 20. PMID:27338640 doi:http://dx.doi.org/10.1016/j.bbrc.2016.06.097
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