7cl4: Difference between revisions
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<StructureSection load='7cl4' size='340' side='right'caption='[[7cl4]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='7cl4' size='340' side='right'caption='[[7cl4]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7cl4]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[7cl4]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_kanamyceticus Streptomyces kanamyceticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CL4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CL4 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</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=7cl4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cl4 OCA], [https://pdbe.org/7cl4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cl4 RCSB], [https://www.ebi.ac.uk/pdbsum/7cl4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cl4 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/KANJ_STRKN KANJ_STRKN] Mediates the conversion of kanamycin B into 2'-dehydrokanamycin A during the transformation of kanamycin B to kanamycin A.<ref>PMID:22374809</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 7cl4" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 7cl4" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Dioxygenase 3D structures|Dioxygenase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Streptomyces kanamyceticus]] | ||
[[Category: Eguchi | [[Category: Eguchi T]] | ||
[[Category: Kitayama | [[Category: Kitayama Y]] | ||
[[Category: Kudo | [[Category: Kudo F]] | ||
[[Category: Miyanaga | [[Category: Miyanaga A]] | ||
Latest revision as of 19:10, 29 November 2023
The crystal structure of KanJ in complex with N-oxalylglycineThe crystal structure of KanJ in complex with N-oxalylglycine
Structural highlights
FunctionKANJ_STRKN Mediates the conversion of kanamycin B into 2'-dehydrokanamycin A during the transformation of kanamycin B to kanamycin A.[1] Publication Abstract from PubMedKanamycin A is the major 2-deoxystreptamine (2DOS)-containing aminoglycoside antibiotic produced by Streptomyces kanamyceticus. The 2DOS moiety is linked with 6-amino-6-deoxy-d-glucose (6ADG) at O-4 and 3-amino-3-deoxy-d-glucose at O-6. Because the 6ADG moiety is derived from d-glucosamine (GlcN), deamination at C-2 and introduction of C-6-NH2 are required in the biosynthesis. A dehydrogenase KanQ and an aminotransferase KanB are presumed to be responsible for the introduction of C-6-NH2, although the substrates have not been identified. Here, we examined the substrate specificity of KanQ to better understand the biosynthetic pathway. It was found that KanQ oxidized kanamycin C more efficiently than the 3-deamino derivative. Furthermore, substrate specificity of an oxygenase KanJ, which is responsible for deamination at C-2 of the GlcN moiety, was examined, and the crystal structure of KanJ was determined. It was found that C-6-NH2 is important for substrate recognition by KanJ. Thus, the modification of the GlcN moiety occurs after pseudotrisaccharide formation, followed by the introduction of C-6-NH2 by KanQ/KanB and deamination at C-2 by KanJ. Stepwise Post-glycosylation Modification of Sugar Moieties in Kanamycin Biosynthesis.,Eguchi T, Kudo F, Kitayama Y, Miyanaga A, Numakura M Chembiochem. 2021 Jan 5. doi: 10.1002/cbic.202000839. PMID:33403742[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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