Acyl carrier protein synthase
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The ''B. subtilis'' AcpS trimer ([[1f80]]) <scene name='3hqj/Acp/2'>binds</scene> three molecules of the acyl carrier protein (ASP). The interactions between ''B. subtilis'' AcpS and ACP are predominantly <scene name='3hqj/Acp/3'>electrostatic</scene>. The ''B. subtilis'' AcpS (white) is shown in spacefill representation, the agrinines, lysines, and histidines are colored <font color='blue'><b>blue</b></font>, while aspartates and glutamates are colored <font color='red'><b>red</b></font>. The ACP molecule (<span style="color:lime;background-color:black;font-weight:bold;">green</span>) is shown in ribbon representation with aspartates and glutamates as sticks and colored <font color='red'><b>red</b></font>. The ''B. subtilis'' AcpS has large <scene name='3hqj/Acp/4'>electropositive interface</scene> with ASP. <scene name='3hqj/Acp/5'>Electrostatic representation</scene> of ''Mtb'' AcpS surface using the similar orientation as ''B. subtilis'' AcpS, shows a moderate electronegative nature in the putative ACP binding site near the <font color='red'><b>ASP 15</b></font>. The ''Mtb'' ASPM structure ([[1klp]], corresponding to ACP) demonstrates considerably lower negative charge. So, the electrostatic interactions between ''Mtb'' AcpS and ASPM are, probably, less important. | The ''B. subtilis'' AcpS trimer ([[1f80]]) <scene name='3hqj/Acp/2'>binds</scene> three molecules of the acyl carrier protein (ASP). The interactions between ''B. subtilis'' AcpS and ACP are predominantly <scene name='3hqj/Acp/3'>electrostatic</scene>. The ''B. subtilis'' AcpS (white) is shown in spacefill representation, the agrinines, lysines, and histidines are colored <font color='blue'><b>blue</b></font>, while aspartates and glutamates are colored <font color='red'><b>red</b></font>. The ACP molecule (<span style="color:lime;background-color:black;font-weight:bold;">green</span>) is shown in ribbon representation with aspartates and glutamates as sticks and colored <font color='red'><b>red</b></font>. The ''B. subtilis'' AcpS has large <scene name='3hqj/Acp/4'>electropositive interface</scene> with ASP. <scene name='3hqj/Acp/5'>Electrostatic representation</scene> of ''Mtb'' AcpS surface using the similar orientation as ''B. subtilis'' AcpS, shows a moderate electronegative nature in the putative ACP binding site near the <font color='red'><b>ASP 15</b></font>. The ''Mtb'' ASPM structure ([[1klp]], corresponding to ACP) demonstrates considerably lower negative charge. So, the electrostatic interactions between ''Mtb'' AcpS and ASPM are, probably, less important. | ||
| - | PPT subtypes are the ''E. coli'' '''ACPS''' and the ''B. subtilis'' '''Sfp'''. For details on Spf see [[Molecular Playground/4'-PHOSPHOPANTETHEINYL TRANSFERASE (Sfp)]]. | + | PPT subtypes are the ''E. coli'' '''ACPS''' and the ''B. subtilis'' '''Sfp'''. For details on Spf see [[Molecular Playground/4'-PHOSPHOPANTETHEINYL TRANSFERASE (Sfp)]]. |
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| - | + | *'''Beta-ketoacyl-acyl carrier protein synthase II''' is involved in temperature controlled fatty acid synthesis<ref>PMID:6988423</ref>. | |
| - | + | See also [[Acyl carrier protein]], [[Fatty acid synthesis]]. | |
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| - | + | ==3D structures of acyl carrier protein synthase== | |
| - | + | [[Acyl carrier protein synthase 3D structures]] | |
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| - | + | </StructureSection> | |
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| - | *ACPS III complex | ||
| - | **[[1hnd]], [[1hnh]], [[2gyo]], [[2eft]] - EcACPS III + CoA<br /> | ||
| - | **[[1hnj]] - EcACPS III + malonyl-CoA<br /> | ||
| - | **[[2qx1]] - EcACPS III + decyl-CoA<br /> | ||
| - | **[[1mzs]], [[5bnm]], [[5bnr]], [[5bns]] - EcACPS III + inhibitor<br /> | ||
| - | **[[5bqs]] - SpACPS III + inhibitor<br /> | ||
| - | **[[4z8d]] - HiACPS III + inhibitor<br /> | ||
| - | **[[1u6s]] - MtACPS III (mutant) + lauroyl-CoA<br /> | ||
| - | **[[2qnx]], [[2qo1]] - MtACPS III + undecanoic acid<br /> | ||
| - | **[[2qo0]] - MtACPS III (mutant) + undecanoic acid<br /> | ||
| - | **[[2qnz]] - MtACPS III + decyl formate<br /> | ||
| - | **[[2qny]] - MtACPS III (mutant) + decyl formate<br /> | ||
| - | **[[1ub7]] - TtACPS III (mutant)<br /> | ||
| - | **[[3il4]] - EfACPS III + CoA – ''Enterococcus faecalis''<br /> | ||
| - | **[[3il5]] - EfACPS III + benzoic acid derivative<br /> | ||
| - | **[[3il6]] - EfACPS III (mutant) + benzoic acid derivative<br /> | ||
| - | **[[4nhd]] - VcACPS III + CoA<br /> | ||
| - | **[[4x0o]] - VcACPS III-2 + acetyl-CoA<br /> | ||
| - | **[[5kp2]], [[5v0p]] - VcACPS III-2 + octanoyl-CoA<br /> | ||
| - | }} | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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References
- Parris KD, Lin L, Tam A, Mathew R, Hixon J, Stahl M, Fritz CC, Seehra J, Somers WS. Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites. Structure. 2000 Aug 15;8(8):883-95. PMID:10997907
- Dym O, Albeck S, Peleg Y, Schwarz A, Shakked Z, Burstein Y, Zimhony O. Structure-function analysis of the acyl carrier protein synthase (AcpS) from Mycobacterium tuberculosis. J Mol Biol. 2009 Nov 6;393(4):937-50. Epub 2009 Sep 3. PMID:19733180 doi:10.1016/j.jmb.2009.08.065
Proteopedia Page Contributors and Editors (what is this?)
Categories: Topic Page | Mycobacterium tuberculosis | Albeck,S. | Burstein,Y. | Dym,O. | ISPC, Israel Structural Proteomics Center. | Peleg,Y. | Schwarz,A. | Shakked,Z. | Zimhony,O. | An/fold | Cytoplasm | Fatty acid biosynthesis | ISPC | Israel Structural Proteomics Center | Lipid synthesis | Magnesium | Metal-binding | Structural genomic | Transferase

