3kg1: Difference between revisions

Latest revision as of 10:16, 21 February 2024

Crystal structure of SnoaB, a cofactor-independent oxygenase from Streptomyces nogalater, mutant N63A

Structural highlights

3kg1 is a 3 chain structure with sequence from Streptomyces nogalater. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Ligands:	CL
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).^[1] ^[2] ^[3] ^[4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ Ylihonko K, Tuikkanen J, Jussila S, Cong L, Mäntsälä P. A gene cluster involved in nogalamycin biosynthesis from Streptomyces nogalater: sequence analysis and complementation of early-block mutations in the anthracycline pathway. Mol Gen Genet. 1996 May 23;251(2):113-20. PMID:8668120 doi:10.1007/BF02172908
↑ Ylihonko K, Hakala J, Kunnari T, Mäntsälä P. Production of hybrid anthracycline antibiotics by heterologous expression of Streptomyces nogalater nogalamycin biosynthesis genes. Microbiology (Reading). 1996 Aug;142 ( Pt 8):1965-72. PMID:8760909 doi:10.1099/13500872-142-8-1965
↑ Koskiniemi H, Grocholski T, Schneider G, Niemi J. Expression, purification and crystallization of the cofactor-independent monooxygenase SnoaB from the nogalamycin biosynthetic pathway. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Mar 1;65(Pt, 3):256-9. Epub 2009 Feb 14. PMID:19255477 doi:10.1107/S1744309109001389
↑ Grocholski T, Koskiniemi H, Lindqvist Y, Mantsala P, Niemi J, Schneider G. Crystal Structure of the Cofactor-Independent Monooxygenase SnoaB from Streptomyces nogalater: Implications for the Reaction Mechanism. Biochemistry. 2010 Jan 12. PMID:20052967 doi:10.1021/bi901985b

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Ylihonko K, Tuikkanen J, Jussila S, Cong L, Mäntsälä P. A gene cluster involved in nogalamycin biosynthesis from Streptomyces nogalater: sequence analysis and complementation of early-block mutations in the anthracycline pathway. Mol Gen Genet. 1996 May 23;251(2):113-20. PMID:8668120 doi:10.1007/BF02172908

[2] Ylihonko K, Hakala J, Kunnari T, Mäntsälä P. Production of hybrid anthracycline antibiotics by heterologous expression of Streptomyces nogalater nogalamycin biosynthesis genes. Microbiology (Reading). 1996 Aug;142 ( Pt 8):1965-72. PMID:8760909 doi:10.1099/13500872-142-8-1965

[3] Koskiniemi H, Grocholski T, Schneider G, Niemi J. Expression, purification and crystallization of the cofactor-independent monooxygenase SnoaB from the nogalamycin biosynthetic pathway. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Mar 1;65(Pt, 3):256-9. Epub 2009 Feb 14. PMID:19255477 doi:10.1107/S1744309109001389

[4] Grocholski T, Koskiniemi H, Lindqvist Y, Mantsala P, Niemi J, Schneider G. Crystal Structure of the Cofactor-Independent Monooxygenase SnoaB from Streptomyces nogalater: Implications for the Reaction Mechanism. Biochemistry. 2010 Jan 12. PMID:20052967 doi:10.1021/bi901985b

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[2]

[3]

[4]

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:3kg1.jpg|left|200px]]
-<!--
+==Crystal structure of SnoaB, a cofactor-independent oxygenase from Streptomyces nogalater, mutant N63A==
-The line below this paragraph, containing "STRUCTURE_3kg1", creates the "Structure Box" on the page.
+<StructureSection load='3kg1' size='340' side='right'caption='[[3kg1]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
--->
+<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>
-{{STRUCTURE_3kg1|  PDB=3kg1  |  SCENE=  }}
+<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>
-===Crystal structure of SnoaB, a cofactor-independent oxygenase from Streptomyces nogalater, mutant N63A===
+== 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 ==
-<!--
+[[Image:Consurf_key_small.gif|200px|right]]
-The line below this paragraph, {{ABSTRACT_PUBMED_20052967}}, adds the Publication Abstract to the page
+Check<jmol>
-(as it appears on PubMed at http://www.pubmed.gov), where 20052967 is the PubMed ID number.
+  <jmolCheckbox>
--->
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kg/3kg1_consurf.spt"</scriptWhenChecked>
-{{ABSTRACT_PUBMED_20052967}}
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
-==About this Structure==
+  </jmolCheckbox>
-KG1 is a 3 chains structure with sequences from [http://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].
+</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>
-==Reference==
+== References ==
-<ref group="xtra">PMID:20052967</ref><ref group="xtra">PMID:19255477</ref><references group="xtra"/>
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Streptomyces nogalater]]
-[[Category: Grocholski, T.]]
+[[Category: Grocholski T]]
-[[Category: Koskiniemi, H.]]
+[[Category: Koskiniemi H]]
-[[Category: Lindqvist, Y.]]
+[[Category: Lindqvist Y]]
-[[Category: Mantsala, P.]]
+[[Category: Mantsala P]]
-[[Category: Niemi, J.]]
+[[Category: Niemi J]]
-[[Category: Schneider, G.]]
+[[Category: Schneider G]]
-[[Category: Anthracycline]]
-[[Category: Cofactor-independent]]
-[[Category: Oxidoreductase]]
-[[Category: Oxygenase]]
-[[Category: Polyketide]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 27 19:35:06 2010''

3kg1: Difference between revisions

Latest revision as of 10:16, 21 February 2024

Crystal structure of SnoaB, a cofactor-independent oxygenase from Streptomyces nogalater, mutant N63A

Structural highlights

Function

Evolutionary Conservation

References

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