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-[[Image:1odo.jpg|left|200px]]<br /><applet load="1odo" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1odo, resolution 1.85&Aring;" />
-'''1.85 A STRUCTURE OF CYP154A1 FROM STREPTOMYCES COELICOLOR A3(2)'''<br />
-==Overview==
+==1.85 A structure of CYP154A1 from Streptomyces coelicolor A3(2)==
-The genus Streptomyces produces two-thirds of microbially derived, antibiotics. Polyketides form the largest and most diverse group of these, natural products. Antibiotic diversity of polyketides is generated during, their biosynthesis by several means, including postpolyketide modification, performed by oxidoreductases, a broad group of enzymes including, cytochrome P450 monooxygenases (CYPs). CYPs catalyze site-specific, oxidation of macrolide antibiotic precursors significantly affecting, antibiotic activity. Efficient manipulation of Streptomyces CYPs in, generating new antibiotics will require identification and/or engineering, of monooxygenases with activities toward a diverse array of chemical, substrates. To begin to link structure to function of CYPs involved in, secondary metabolic pathways of industrially important species, we, determined the X-ray structure of Streptomyces coelicolor A3(2) CYP154A1, at 1.85 A and analyzed it in the context of the closely related CYP154C1, and more distant CYPs from polyketide synthase (EryF) and nonribosomal, peptide synthetase (OxyB) biosynthetic pathways. In contrast to CYP154C1, CYP154A1 reveals an active site inaccessible from the molecular surface, and an absence of catalytic activities observed for CYP154C1. Systematic, variations in the amino acid patterns and length of the surface HI loop, correlate with degree of rotation of the F and G helices relative to the, active site in CYP154A1-related CYPs, presumably regulating the degree of, active site accessibility and its dimensions. Heme in CYP154A1 is in a 180, degrees flipped orientation compared with most other structurally, determined CYPs.
+<StructureSection load='1odo' size='340' side='right'caption='[[1odo]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1odo]] 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=1ODO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ODO FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PIM:4-PHENYL-1H-IMIDAZOLE'>PIM</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=1odo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1odo OCA], [https://pdbe.org/1odo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1odo RCSB], [https://www.ebi.ac.uk/pdbsum/1odo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1odo ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q9KZR7_STRCO Q9KZR7_STRCO]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/od/1odo_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1odo ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The genus Streptomyces produces two-thirds of microbially derived antibiotics. Polyketides form the largest and most diverse group of these natural products. Antibiotic diversity of polyketides is generated during their biosynthesis by several means, including postpolyketide modification performed by oxidoreductases, a broad group of enzymes including cytochrome P450 monooxygenases (CYPs). CYPs catalyze site-specific oxidation of macrolide antibiotic precursors significantly affecting antibiotic activity. Efficient manipulation of Streptomyces CYPs in generating new antibiotics will require identification and/or engineering of monooxygenases with activities toward a diverse array of chemical substrates. To begin to link structure to function of CYPs involved in secondary metabolic pathways of industrially important species, we determined the X-ray structure of Streptomyces coelicolor A3(2) CYP154A1 at 1.85 A and analyzed it in the context of the closely related CYP154C1 and more distant CYPs from polyketide synthase (EryF) and nonribosomal peptide synthetase (OxyB) biosynthetic pathways. In contrast to CYP154C1, CYP154A1 reveals an active site inaccessible from the molecular surface, and an absence of catalytic activities observed for CYP154C1. Systematic variations in the amino acid patterns and length of the surface HI loop correlate with degree of rotation of the F and G helices relative to the active site in CYP154A1-related CYPs, presumably regulating the degree of active site accessibility and its dimensions. Heme in CYP154A1 is in a 180 degrees flipped orientation compared with most other structurally determined CYPs.
-==About this Structure==
+Comparison of the 1.85 A structure of CYP154A1 from Streptomyces coelicolor A3(2) with the closely related CYP154C1 and CYPs from antibiotic biosynthetic pathways.,Podust LM, Bach H, Kim Y, Lamb DC, Arase M, Sherman DH, Kelly SL, Waterman MR Protein Sci. 2004 Jan;13(1):255-68. PMID:14691240<ref>PMID:14691240</ref>
-ODO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=PIM:'>PIM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Pim+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ODO OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Comparison of the 1.85 A structure of CYP154A1 from Streptomyces coelicolor A3(2) with the closely related CYP154C1 and CYPs from antibiotic biosynthetic pathways., Podust LM, Bach H, Kim Y, Lamb DC, Arase M, Sherman DH, Kelly SL, Waterman MR, Protein Sci. 2004 Jan;13(1):255-68. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14691240 14691240]
+</div>
-[[Category: Single protein]]
+<div class="pdbe-citations 1odo" style="background-color:#fffaf0;"></div>
-[[Category: Streptomyces coelicolor]]
+== References ==
-[[Category: Arase, M.]]
+<references/>
-[[Category: Bach, H.]]
+__TOC__
-[[Category: Kelly, S.L.]]
+</StructureSection>
-[[Category: Kim, Y.]]
+[[Category: Large Structures]]
-[[Category: Lamb, D.C.]]
+[[Category: Arase M]]
-[[Category: Podust, L.M.]]
+[[Category: Bach H]]
-[[Category: Sherman, D.H.]]
+[[Category: Kelly SL]]
-[[Category: Waterman, M.R.]]
+[[Category: Kim Y]]
-[[Category: HEM]]
+[[Category: Lamb DC]]
-[[Category: PIM]]
+[[Category: Podust LM]]
-[[Category: cytochrome]]
+[[Category: Sherman DH]]
-[[Category: oxidoreductase]]
+[[Category: Waterman MR]]
-[[Category: p450 monooxygenase]]
-[[Category: streptomyces]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:56:40 2008''