1af8

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[[Image:1af8.gif|left|200px]]<br /><applet load="1af8" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1af8" />
 
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'''ACTINORHODIN POLYKETIDE SYNTHASE ACYL CARRIER PROTEIN FROM STREPTOMYCES COELICOLOR A3(2), NMR, 24 STRUCTURES'''<br />
 
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==Overview==
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==ACTINORHODIN POLYKETIDE SYNTHASE ACYL CARRIER PROTEIN FROM STREPTOMYCES COELICOLOR A3(2), NMR, 24 STRUCTURES==
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The solution structure of the actinorhodin acyl carrier protein (act apo-ACP) from the polyketide synthase (PKS) of Streptomyces coelicolor A3(2) has been determined using 1H NMR spectroscopy, representing the first polyketide synthase component for which detailed structural information has been obtained. Twenty-four structures were generated by simulated annealing, employing 699 distance restraints and 94 dihedral angle restraints. The structure is composed, principally, of three major helices (1, 2, and 4), a shorter helix (3) and a large loop region separating helices 1 and 2. The structure is well-defined, except for a portion of the loop region (residues 18-29), the N-terminus (1-4), and a short stretch (57-61) in the loop connecting helices 2 and 3. The RMS distribution of the 24 structures about the average structure is 1.47 A for backbone atoms, 1.84 A for all heavy atoms (residues 5-86), and 1.01 A for backbone atoms over the helical regions (5-18, 41-86). The tertiary fold of act apo-ACP shows a strong structural homology with Escherichia coli fatty acid synthase (FAS) ACP, though some structural differences exist. First, there is no evidence that act apo-ACP is conformationally averaged between two or more states as observed in E. coli FAS ACP. Second, act apo-ACP shows a disordered N-terminus (residues 1-4) and a longer flexible loop (19-41 with 19-29 disordered) as opposed to E. coli FAS ACP where the N-terminal helix starts at residue 3 and the loop region is three amino acids shorter (16-35). Most importantly, however, although the act apo-ACP structure contains a hydrophobic core, there are in addition a number of buried hydrophilic groups, principally Arg72 and Asn79, both of which are 100% conserved in the PKS ACPs and not the FAS ACPs and may therefore play a role in stabilizing the growing polyketide chain. The structure-function relationship of act ACP is discussed in the light of these structural data and recent genetic advances in the field.
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<StructureSection load='1af8' size='340' side='right'caption='[[1af8]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1af8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor_A3(2) Streptomyces coelicolor A3(2)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AF8 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1af8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1af8 OCA], [https://pdbe.org/1af8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1af8 RCSB], [https://www.ebi.ac.uk/pdbsum/1af8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1af8 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ACPX_STRCO ACPX_STRCO] Acyl carrier protein.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/af/1af8_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1af8 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1AF8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Known structural/functional Site: <scene name='pdbsite=S42:Attachment+Site+Of+Phosphopantatheine+Prosthetic+Group+I+...'>S42</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AF8 OCA].
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*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Solution structure of the actinorhodin polyketide synthase acyl carrier protein from Streptomyces coelicolor A3(2)., Crump MP, Crosby J, Dempsey CE, Parkinson JA, Murray M, Hopwood DA, Simpson TJ, Biochemistry. 1997 May 20;36(20):6000-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9166770 9166770]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Crosby J]]
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[[Category: Streptomyces coelicolor]]
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[[Category: Crump MP]]
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[[Category: Crosby, J.]]
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[[Category: Dempsey CE]]
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[[Category: Crump, M P.]]
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[[Category: Hopwood DA]]
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[[Category: Dempsey, C E.]]
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[[Category: Murray M]]
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[[Category: Hopwood, D A.]]
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[[Category: Parkinson JA]]
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[[Category: Murray, M.]]
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[[Category: Simpson TJ]]
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[[Category: Parkinson, J A.]]
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[[Category: Simpson, T J.]]
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[[Category: acyl carrier protein]]
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[[Category: antibiotic biosynthesis]]
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[[Category: nmr structure]]
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[[Category: polyketide]]
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[[Category: solution structure]]
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[[Category: streptomyces]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:43:54 2008''
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Current revision

ACTINORHODIN POLYKETIDE SYNTHASE ACYL CARRIER PROTEIN FROM STREPTOMYCES COELICOLOR A3(2), NMR, 24 STRUCTURES

PDB ID 1af8

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