This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

7cl2

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

The crystal structure of KanJ

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7cl2"

@@ Line 3: / Line 3: @@
 <StructureSection load='7cl2' size='340' side='right'caption='[[7cl2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[7cl2]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/As_4.1441 As 4.1441]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CL2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CL2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7cl2]] 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=7CL2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CL2 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">kanJ, kacB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1967 AS 4.1441])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.37 1.14.11.37] </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=7cl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cl2 OCA], [https://pdbe.org/7cl2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cl2 RCSB], [https://www.ebi.ac.uk/pdbsum/7cl2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cl2 ProSAT]</span></td></tr>
 </table>
 == 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>
+[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;">
-== Publication Abstract from PubMed ==
-Kanamycin 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<ref>PMID:33403742</ref>
+==See Also==
+*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 7cl2" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: As 4 1441]]
 [[Category: Large Structures]]
-[[Category: Oxidoreductase]]
+[[Category: Streptomyces kanamyceticus]]
-[[Category: Eguchi, T]]
+[[Category: Eguchi T]]
-[[Category: Kitayama, Y]]
+[[Category: Kitayama Y]]
-[[Category: Kudo, F]]
+[[Category: Kudo F]]
-[[Category: Miyanaga, A]]
+[[Category: Miyanaga A]]
-[[Category: Dioxygenase]]
-[[Category: Kanamycin biosynthesis]]

7cl2

From Proteopedia

Current revision

The crystal structure of KanJ

Structural highlights

Function

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox