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[[Image:1s1f.gif|left|200px]]<br /><applet load="1s1f" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1s1f, resolution 1.50&Aring;" />
'''Crystal Structure of Streptomyces Coelicolor A3(2) CYP158A2 from antibiotic biosynthetic pathways'''<br />


==Overview==
==Crystal Structure of Streptomyces Coelicolor A3(2) CYP158A2 from antibiotic biosynthetic pathways==
Cytochrome P450 158A2 (CYP158A2) is encoded within a three-gene operon (sco1206-sco1208) in the prototypic soil bacterium Streptomyces coelicolor A3(2). This operon is widely conserved among streptomycetes. CYP158A2 has been suggested to produce polymers of flaviolin, a pigment that may protect microbes from UV radiation, in combination with the adjacent rppA gene, which encodes the type III polyketide synthase, 1,3,6,8-tetrahydroxynaphthalene synthase. Following cloning, expression, and purification of this cytochrome P450, we have shown that it can produce dimer and trimer products from the substrate flaviolin and that the structures of two of the dimeric products were established using mass spectrometry and multiple NMR methods. A comparison of the x-ray structures of ligand-free (1.75 angstroms) and flaviolin-bound (1.62 angstroms) forms of CYP158A2 demonstrates a major conformational change upon ligand binding that closes the entry into the active site, partly due to repositioning of the F and G helices. Particularly interesting is the presence of two molecules of flaviolin in the closed active site. The flaviolin molecules form a quasi-planar three-molecule stack including the heme of CYP158A2, suggesting that oxidative C-C coupling of these phenolic molecules leads to the production of flaviolin dimers.
<StructureSection load='1s1f' size='340' side='right'caption='[[1s1f]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1s1f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor_A3(2) Streptomyces coelicolor A3(2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S1F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S1F FirstGlance]. <br>
1S1F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria] with <scene name='pdbligand=HG:'>HG</scene>, <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=PIM:'>PIM</scene>, <scene name='pdbligand=MLA:'>MLA</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S1F OCA].
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=PIM:4-PHENYL-1H-IMIDAZOLE'>PIM</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1s1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s1f OCA], [https://pdbe.org/1s1f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s1f RCSB], [https://www.ebi.ac.uk/pdbsum/1s1f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s1f ProSAT]</span></td></tr>
Binding of two flaviolin substrate molecules, oxidative coupling, and crystal structure of Streptomyces coelicolor A3(2) cytochrome P450 158A2., Zhao B, Guengerich FP, Bellamine A, Lamb DC, Izumikawa M, Lei L, Podust LM, Sundaramoorthy M, Kalaitzis JA, Reddy LM, Kelly SL, Moore BS, Stec D, Voehler M, Falck JR, Shimada T, Waterman MR, J Biol Chem. 2005 Mar 25;280(12):11599-607. Epub 2005 Jan 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15659395 15659395]
</table>
[[Category: Bacteria]]
== Function ==
[[Category: Single protein]]
[https://www.uniprot.org/uniprot/C1582_STRCO C1582_STRCO] Catalyze oxidative C-C coupling reaction to polymerize flaviolin and form highly conjugated pigments which protect the soil bacterium from deleterious effects of UV irradiation (three isomers of biflaviolin and one triflaviolin).<ref>PMID:15659395</ref> <ref>PMID:16239228</ref>
[[Category: Lamb, D C.]]
== Evolutionary Conservation ==
[[Category: Lei, L.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Podust, L M.]]
Check<jmol>
[[Category: Sundaramoorthy, M.]]
  <jmolCheckbox>
[[Category: Waterman, M R.]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s1/1s1f_consurf.spt"</scriptWhenChecked>
[[Category: Zhao, B.]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: GOL]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: HEM]]
  </jmolCheckbox>
[[Category: HG]]
</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=1s1f ConSurf].
[[Category: MLA]]
<div style="clear:both"></div>
[[Category: PIM]]
== References ==
[[Category: antibiotic biosynthesis]]
<references/>
[[Category: cyp158a2]]
__TOC__
[[Category: cytochrome p450 oxidoreductase]]
</StructureSection>
[[Category: streptomyces]]
[[Category: Large Structures]]
 
[[Category: Lamb DC]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:56:57 2008''
[[Category: Lei L]]
[[Category: Podust LM]]
[[Category: Sundaramoorthy M]]
[[Category: Waterman MR]]
[[Category: Zhao B]]

Latest revision as of 11:27, 14 February 2024

Crystal Structure of Streptomyces Coelicolor A3(2) CYP158A2 from antibiotic biosynthetic pathwaysCrystal Structure of Streptomyces Coelicolor A3(2) CYP158A2 from antibiotic biosynthetic pathways

Structural highlights

1s1f is a 1 chain structure with sequence from Streptomyces coelicolor A3(2). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.5Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

C1582_STRCO Catalyze oxidative C-C coupling reaction to polymerize flaviolin and form highly conjugated pigments which protect the soil bacterium from deleterious effects of UV irradiation (three isomers of biflaviolin and one triflaviolin).[1] [2]

Evolutionary Conservation

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

References

  1. ↑ Zhao B, Guengerich FP, Bellamine A, Lamb DC, Izumikawa M, Lei L, Podust LM, Sundaramoorthy M, Kalaitzis JA, Reddy LM, Kelly SL, Moore BS, Stec D, Voehler M, Falck JR, Shimada T, Waterman MR. Binding of two flaviolin substrate molecules, oxidative coupling, and crystal structure of Streptomyces coelicolor A3(2) cytochrome P450 158A2. J Biol Chem. 2005 Mar 25;280(12):11599-607. Epub 2005 Jan 19. PMID:15659395 doi:http://dx.doi.org/10.1074/jbc.M410933200
  2. ↑ Zhao B, Guengerich FP, Voehler M, Waterman MR. Role of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: a new mechanism of proton transfer. J Biol Chem. 2005 Dec 23;280(51):42188-97. Epub 2005 Oct 20. PMID:16239228 doi:10.1074/jbc.M509220200

1s1f, resolution 1.50Å

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