3kg1
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='3kg1' size='340' side='right'caption='[[3kg1]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='3kg1' size='340' side='right'caption='[[3kg1]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3kg1]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3kg1]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_nogalater Streptomyces nogalater]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KG1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KG1 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]] 2.5Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=3kg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kg1 OCA], [https://pdbe.org/3kg1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kg1 RCSB], [https://www.ebi.ac.uk/pdbsum/3kg1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kg1 ProSAT]</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=3kg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kg1 OCA], [https://pdbe.org/3kg1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kg1 RCSB], [https://www.ebi.ac.uk/pdbsum/3kg1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kg1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SNOAB_STRNO SNOAB_STRNO] Involved in the biosynthesis of the anthracycline (aromatic polyketide) antibiotic nogalamycin (PubMed:8760909, PubMed:8668120). Catalyzes the oxygenation of 12-deoxy-nogalonic acid at position 12 to yield nogalonic acid (PubMed:19255477, PubMed:20052967).<ref>PMID:8668120</ref> <ref>PMID:8760909</ref> <ref>PMID:19255477</ref> <ref>PMID:20052967</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 19: | Line 20: | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3kg1 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3kg1 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | SnoaB is a cofactor-independent monooxygenase that catalyzes the conversion of 12-deoxynogalonic acid to nogalonic acid in the biosynthesis of the aromatic polyketide nogalamycin in Streptomyces nogalater. In vitro (18)O(2) experiments establish that the oxygen atom incorporated into the substrate is derived from molecular oxygen. The crystal structure of the enzyme was determined in two different space groups to 1.7 and 1.9 A resolution, respectively. The enzyme displays the ferredoxin fold, with the characteristic beta-strand exchange at the dimer interface. The crystal structures reveal a putative catalytic triad involving two asparagine residues, Asn18 and Asn63, and a water molecule, which may play important roles in the enzymatic reaction. Site-directed mutagenesis experiments, replacing the two asparagines individually by alanine, led to a 100-fold drop in enzymatic activity. Replacement of an invariant tryptophan residue in the active site of the enzyme by phenylalanine also resulted in an enzyme variant with about 1% residual activity. Taken together, our findings are most consistent with a carbanion mechanism where the deprotonated substrate reacts with molecular oxygen via one electron transfer and formation of a caged radical. | ||
| - | |||
| - | Crystal Structure of the Cofactor-Independent Monooxygenase SnoaB from Streptomyces nogalater: Implications for the Reaction Mechanism.,Grocholski T, Koskiniemi H, Lindqvist Y, Mantsala P, Niemi J, Schneider G Biochemistry. 2010 Jan 12. PMID:20052967<ref>PMID:20052967</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3kg1" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: As 4 1442]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Grocholski | + | [[Category: Streptomyces nogalater]] |
| - | [[Category: Koskiniemi | + | [[Category: Grocholski T]] |
| - | [[Category: Lindqvist | + | [[Category: Koskiniemi H]] |
| - | [[Category: Mantsala | + | [[Category: Lindqvist Y]] |
| - | [[Category: Niemi | + | [[Category: Mantsala P]] |
| - | [[Category: Schneider | + | [[Category: Niemi J]] |
| - | + | [[Category: Schneider G]] | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Crystal structure of SnoaB, a cofactor-independent oxygenase from Streptomyces nogalater, mutant N63A
| |||||||||||
