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4kwh

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Revision as of 15:28, 11 August 2016

The crystal structure of angucycline C-6 ketoreductase LanV with bound NADP

Structural highlights

4kwh is a 2 chain structure with sequence from "actinomyces_cyanogenus"_krasil'nikov_et_al. "actinomyces cyanogenus" krasil'nikov et al.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	4kwi
Gene:	lanV ("Actinomyces cyanogenus" Krasil'nikov et al.)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Angucyclines are biologically active natural products constructed around a common benz[a]anthraquinone carbon frame. One key branching point in the biosynthesis of angucyclines is the ketoreduction at C-6, which results in the opposite stereochemistry of landomycins and urdamycins/gaudimycins. Here we present the 1.65 A resolution crystal structure of LanV from Streptomyces cyanogenus S136 that is responsible for the 6R stereochemistry of landomycins. The enzyme displays the common architectural fold of short-chain alcohol dehydrogenases/reductases and contains bound nicotinamide adenine dinucleotide phosphate. Determination of the structure of LanV in complex with 11-deoxylandomycinone at 2.0 A resolution indicated that substrate binding does not induce large conformational changes and that substrate recognition occurs mainly through hydrophobic interactions. Analysis of the electron density map of the ternary complex revealed that the catalytic reaction had most likely proceeded backward in the crystal, because the data could be best fit with a compound harboring a carbonyl group at C-6. A coordinated water molecule was atypically identified between the ligand and the conserved Tyr160 residue, which was confirmed to be critical for the catalytic activity by site-directed mutagenesis. A catalytic triad of Ser147, Tyr160, and Lys164 could be recognized on the basis of the crystal structure, and stereoselective labeling studies demonstrated that the transfer of hydride from reduced nicotinamide adenine dinucleotide phosphate to the substrate occurs from the 4-pro-S side of the cosubstrate. Importantly, Ser192 was identified as being involved in controlling the stereochemistry of the reaction, as assays with single mutant Ser192Ile led to accumulation of gaudimycin C with 6S stereochemistry as a minor product.

Structural and Functional Analysis of Angucycline C-6 Ketoreductase LanV Involved in Landomycin Biosynthesis.,Paananen P, Patrikainen P, Kallio P, Mantsala P, Niemi J, Niiranen L, Metsa-Ketela M Biochemistry. 2013 Jul 24. PMID:23848284^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Paananen P, Patrikainen P, Kallio P, Mantsala P, Niemi J, Niiranen L, Metsa-Ketela M. Structural and Functional Analysis of Angucycline C-6 Ketoreductase LanV Involved in Landomycin Biosynthesis. Biochemistry. 2013 Jul 24. PMID:23848284 doi:10.1021/bi400712q

1 Structural highlights
2 Publication Abstract from PubMed
3 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4kwh"

@@ Line 1: / Line 1: @@
 ==The crystal structure of angucycline C-6 ketoreductase LanV with bound NADP==
 <StructureSection load='4kwh' size='340' side='right' caption='[[4kwh]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kwi|4kwi]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lanV ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=80860 "Actinomyces cyanogenus" Krasil'nikov et al.])</td></tr>
-<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=4kwh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kwh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kwh RCSB], [http://www.ebi.ac.uk/pdbsum/4kwh PDBsum]</span></td></tr>
+<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=4kwh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kwh OCA], [http://pdbe.org/4kwh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kwh RCSB], [http://www.ebi.ac.uk/pdbsum/4kwh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kwh ProSAT]</span></td></tr>
 </table>
 <div style="background-color:#fffaf0;">
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4kwh" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4kwh

From Proteopedia

Revision as of 15:28, 11 August 2016

The crystal structure of angucycline C-6 ketoreductase LanV with bound NADP

Structural highlights

Publication Abstract from PubMed

References

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