|
|
| (3 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | + | |
| | ==The actinorhodin apo acyl carrier protein from S. coelicolor== | | ==The actinorhodin apo acyl carrier protein from S. coelicolor== |
| - | <StructureSection load='2k0y' size='340' side='right' caption='[[2k0y]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2k0y' size='340' side='right'caption='[[2k0y]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2k0y]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K0Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K0Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2k0y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K0Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K0Y FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1af8|1af8]], [[2af8|2af8]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2k0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k0y OCA], [http://pdbe.org/2k0y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k0y RCSB], [http://www.ebi.ac.uk/pdbsum/2k0y PDBsum]</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=2k0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k0y OCA], [https://pdbe.org/2k0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k0y RCSB], [https://www.ebi.ac.uk/pdbsum/2k0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k0y ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ACPX_STRCO ACPX_STRCO]] Acyl carrier protein. | + | [https://www.uniprot.org/uniprot/ACPX_STRCO ACPX_STRCO] Acyl carrier protein. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k0/2k0y_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k0/2k0y_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| Line 31: |
Line 32: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Streptomyces coelicolor]] | | [[Category: Streptomyces coelicolor]] |
| - | [[Category: Christopher, W]] | + | [[Category: Christopher W]] |
| - | [[Category: Crump, M P]] | + | [[Category: Crump MP]] |
| - | [[Category: Evans, S E]] | + | [[Category: Evans SE]] |
| - | [[Category: Actinorhodin]]
| + | |
| - | [[Category: Acyl carrier protein]]
| + | |
| - | [[Category: Antibiotic]]
| + | |
| - | [[Category: Antibiotic biosynthesis]]
| + | |
| - | [[Category: Phosphopantetheine]]
| + | |
| - | [[Category: Polyketide]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
ACPX_STRCO Acyl carrier protein.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The actinorhodin (act) synthase acyl carrier protein (ACP) from Streptomyces coelicolor plays a central role in polyketide biosynthesis. Polyketide intermediates are bound to the free sulfhydryl group of a phosphopantetheine arm that is covalently linked to a conserved serine residue in the holo form of the ACP. The solution NMR structures of both the apo and holo forms of the ACP are reported, which represents the first high resolution comparison of these two forms of an ACP. Ensembles of twenty apo and holo structures were calculated and yielded atomic root mean square deviations of well-ordered backbone atoms to the average coordinates of 0.37 and 0.42 A, respectively. Three restraints defining the protein to the phosphopantetheine interface were identified. Comparison of the apo and holo forms revealed previously undetected conformational changes. Helix III moved towards helix II (contraction of the ACP), and Leu43 on helix II subtly switched from being solvent exposed to forming intramolecular interactions with the newly added phosphopantetheine side chain. Tryptophan fluorescence and S. coelicolor fatty acid synthase (FAS) holo-synthase (ACPS) assays indicated that apo-ACP has a twofold higher affinity (K(d) of 1.1 muM) than holo-ACP (K(d) of 2.1 muM) for ACPS. Site-directed mutagenesis of Leu43 and Asp62 revealed that both mutations affect binding, but have differential affects on modification by ACPS. Leu43 mutations in particular strongly modulate binding affinity for ACPS. Comparison of apo- and holo-ACP structures with known models of the Bacillus subtilis FAS ACP-holo-acyl carrier protein synthase (ACPS) complex suggests that conformational modulation of helix II and III between apo- and holo-ACP could play a role in dissociation of the ACP-ACPS complex.
An ACP Structural Switch: Conformational Differences between the Apo and Holo Forms of the Actinorhodin Polyketide Synthase Acyl Carrier Protein.,Evans SE, Williams C, Arthur CJ, Burston SG, Simpson TJ, Crosby J, Crump MP Chembiochem. 2008 Sep 3. PMID:18770515[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Evans SE, Williams C, Arthur CJ, Burston SG, Simpson TJ, Crosby J, Crump MP. An ACP Structural Switch: Conformational Differences between the Apo and Holo Forms of the Actinorhodin Polyketide Synthase Acyl Carrier Protein. Chembiochem. 2008 Sep 3. PMID:18770515 doi:10.1002/cbic.200800180
|
