3rbv

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==Crystal Structure of KijD10, a 3-ketoreductase from Actinomadura kijaniata incomplex with NADP==
==Crystal Structure of KijD10, a 3-ketoreductase from Actinomadura kijaniata incomplex with NADP==
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<StructureSection load='3rbv' size='340' side='right' caption='[[3rbv]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<StructureSection load='3rbv' size='340' side='right'caption='[[3rbv]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3rbv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Actinomadura_kijaniata Actinomadura kijaniata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RBV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RBV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3rbv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinomadura_kijaniata Actinomadura kijaniata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RBV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RBV 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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.9&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rc1|3rc1]], [[3rc2|3rc2]], [[3rc7|3rc7]], [[3rc9|3rc9]], [[3rcb|3rcb]]</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KijD10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=46161 Actinomadura kijaniata])</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=3rbv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rbv OCA], [https://pdbe.org/3rbv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rbv RCSB], [https://www.ebi.ac.uk/pdbsum/3rbv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rbv 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=3rbv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rbv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rbv RCSB], [http://www.ebi.ac.uk/pdbsum/3rbv PDBsum]</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/KIJDR_ACTKI KIJDR_ACTKI] Involved in the biosynthesis of L-digitoxose, an unusual dideoxysugar attached to various pharmacologically active natural products, including the antitumor antibiotic tetrocarcin A, and the antibiotics kijanimicin and jadomycin B. Catalyzes the reduction of the C-3 keto moiety of dTDP-3,4-diketo-2,6-dideoxy-alpha-D-glucose to yield dTDP-4-keto-2,6-dideoxy-alpha-D-glucose. Also able to reduce dTDP-3-keto-6-deoxy-D-galactose and dTDP-3-keto-6-deoxy-D-glucose to yield dTDP-fucose and dTDP-quinovose, respectively.<ref>PMID:21598943</ref>
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L-digitoxose is an unusual dideoxysugar found attached to various pharmacologically active natural products including the antitumor antibiotic tetrocarcin A, and the antibiotics kijanimicin and jadomycin B. Six enzymes are required for its production starting from glucose-1-phosphate. Here we describe a combined structural and functional investigation of KijD10, an NADPH-dependent C-3'' ketoreductase that catalyzes the third step of L-digitoxose biosynthesis in the African soil-dwelling bacterium Actinomadura kijaniata. KijD10 belongs to the glucose-fructose oxidoreductase (GFOR) superfamily. For this investigation both binary and ternary complexes of KijD10 were crystallized, and their structures determined to 2.0 A resolution or better. On the basis of these high resolution structures, two potential active site acids were identified, Lys 102 and Tyr 186. These residues were individually mutated, and the resultant proteins investigated both kinetically and structurally. The Y186F mutant protein demonstrated significant catalytic activity, and its structure was virtually identical to that of the wild-type enzyme except for the positioning of the nicotinamide ring. All lysine mutations, on the other hand, resulted in proteins with either abolished or drastically reduced catalytic activities. Structures for the K102A and K102E mutant proteins were determined and showed that the abrogation in catalytic activity was not a result of large conformational changes. Taken together these data suggest that Lys 102 donates a proton to the C-3'' hydroxyl group during the reaction and that Tyr 186 serves only an auxiliary role. This is in contrast to that proposed for glucose-fructose oxidoreductase and other family members where the tyrosines, or in some cases similarly positioned histidines, are thought to play major catalytic roles.
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A Combined Structural and Functional Investigation of a C-3''-Ketoreductase Involved in the Biosynthesis of dTDP-L-Digitoxose.,Kubiak RL, Holden HM Biochemistry. 2011 May 20. PMID:21598943<ref>PMID:21598943</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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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Actinomadura kijaniata]]
[[Category: Actinomadura kijaniata]]
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[[Category: Holden, H M]]
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[[Category: Large Structures]]
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[[Category: Kubiak, R L]]
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[[Category: Holden HM]]
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[[Category: Ketoreductase]]
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[[Category: Kubiak RL]]
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[[Category: Nadp binding]]
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[[Category: Sugar binding protein]]
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[[Category: Sugar biosynthesis]]
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Current revision

Crystal Structure of KijD10, a 3-ketoreductase from Actinomadura kijaniata incomplex with NADP

PDB ID 3rbv

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