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Acyl carrier protein synthase

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<StructureSection load='3hqj' size='350' scene='3hqj/Trimer/1' caption="Acyl carrier protein synthase complex with CoA and Mg+2 ion (cyan) [[3hqj]]" >
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<StructureSection load='' size='350' scene='3hqj/Trimer/1' caption="Acyl carrier protein synthase complex with CoA and Mg+2 ion (cyan) [[3hqj]]" >
The crystal structure of '''Acyl carrier protein synthase (AcpS)''' from [http://http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis ''Mycobacterium tuberculosis''] (''Mtb'') was solved at 1.95 Å ([[3hqj]]). It crystallized as one <scene name='3hqj/Trimer/2'>monomer</scene> per asymmetric unit. Since ''Mtb'' AcpS has biologically active trimeric arrangement, <scene name='3hqj/Trimer/3'>AcpS trimer</scene> (in <span style="color:lime;background-color:black;font-weight:bold;">green</span>, <font color='blue'><b>blue</b></font>, and <scene name='3hqj/Trimer/3'>AcpS trimer</scene> (in <span style="color:orange;background-color:black;font-weight:bold;">orange</span>) was constructed using the 3-fold crystallographic symmetry in the ''P''23 space group.
The crystal structure of '''Acyl carrier protein synthase (AcpS)''' from [http://http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis ''Mycobacterium tuberculosis''] (''Mtb'') was solved at 1.95 Å ([[3hqj]]). It crystallized as one <scene name='3hqj/Trimer/2'>monomer</scene> per asymmetric unit. Since ''Mtb'' AcpS has biologically active trimeric arrangement, <scene name='3hqj/Trimer/3'>AcpS trimer</scene> (in <span style="color:lime;background-color:black;font-weight:bold;">green</span>, <font color='blue'><b>blue</b></font>, and <scene name='3hqj/Trimer/3'>AcpS trimer</scene> (in <span style="color:orange;background-color:black;font-weight:bold;">orange</span>) was constructed using the 3-fold crystallographic symmetry in the ''P''23 space group.
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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.
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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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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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</StructureSection>
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==3D structures of acyl carrier protein synthase==
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*'''Beta-ketoacyl-acyl carrier protein synthase II''' is involved in temperature controlled fatty acid synthesis<ref>PMID:6988423</ref>.
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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See also [[Acyl carrier protein]], [[Fatty acid synthesis]].
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*ACPS
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==3D structures of acyl carrier protein synthase==
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[[Acyl carrier protein synthase 3D structures]]
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**[[1af8]], [[2af8]], [[2kg8]], [[2kg9]], [[2kga]], [[2kgc]], [[2kgd]], [[2kge]] – ScACPS – ''Streptomyces coelicolor'' – NMR<br />
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**[[2jca]] - ScACPS <br />
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</StructureSection>
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**[[1fte]], [[1ftf]] - SpACPS – ''Streptococcus pneumoniae''<br />
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**[[1f7l]], [[1f7t]] - BsACPS (mutant) – ''Bacillus subtilis''<br />
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**[[4jm7]] - SaACPS – ''Staphylococcus aureus''<br />
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**[[3hqj]], [[3h7q]], [[3ne1]], [[3ne3]], [[3ne9]], [[3nfd]] - MtACPS – ''Mycobacterium tuberculosis''<br />
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**[[4hc6]] – MtACPS<br />
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**[[3gwm]] - ACPS – ''Mycobacterium smegmatis''<br />
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**[[3qmn]] - VcACPS – ''Vibrio cholera''<br />
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**[[5cxd]] – ACPS – ''Staphylococcus aureus''<br />
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*ACPS complex
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**[[2jbz]] - ScACPS + CoA<br />
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**[[2wds]], [[2wdy]] - ScACPS (mutant) + CoA<br />
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**[[2wdo]] - ScACPS + acetyl-CoA<br />
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**[[1fth]] – SpACPS + ADP<br />
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**[[1f80]] - BsACPS (mutant) + ACP<br />
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**[[2qg8]] - ACPS + ADP – ''Plasmodium yoelii''<br />
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**[[4dxe]] - SaACPS + ACP<br />
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**[[3hyk]] - ACPS + ADP – ''Bacillus anthracis''
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*β-ketoacyl-ACPS
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**[[1w0i]] - AtACPS – ''Arabidopsis thaliana''<br />
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**[[2ix4]] - AtACPS + hexanoic acid<br />
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**[[2c9h]], [[2iwy]], [[3hhd]] – hACPS – human<br />
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**[[2iwz]] - hACPS + hexanoic acid<br />
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*β-ketoacyl-ACPS I
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**[[1dd8]], [[1g5x]], [[2buh]], [[2aq7]], [[2vb7]], [[2vb9]] - EcACPS I - ''Escherichia coli''<br />
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**[[1h4f]], [[2byw]], [[2byy]], [[2bz4]] - EcACPS I (mutant)<br />
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**[[2wgd]] - MtACPS I <br />
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**[[2wgf]] - MtACPS I (mutant)<br />
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**[[2was]] - yACPS I PPT domain – yeast<br />
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**[[3oyt]] - YpACPS I – ''Yersinia psetis''<br />
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**[[4xox]] – VcACPS I<br />
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*ACPS I complex
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**[[1fj4]], [[1fj8]], [[2aqb]], [[2vb8]] - EcACPS I + antibiotic<br />
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**[[2vba]] - EcACPS I + inhibitor<br />
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**[[1ek4]] - EcACPS I (mutant) + dodecanoic acid<br />
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**[[2bui]] - EcACPS I + octanoic acid<br />
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**[[1f91]], [[2byx]], [[2byz]], [[2bz3]] - EcACPS I (mutant) + fatty acid substrate<br />
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**[[2wge]], [[5ld8]] - MtACPS I + antibiotic<br />
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**[[2wgg]] - MtACPS I (mutant) + antibiotic<br />
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**[[4c6u]], [[4c6v]], [[4c6w]], [[4c6x]], [[4c6z]], [[4c70]], [[4c71]], [[4c72]], [[4c73]] - MtACPS I + inhibitor<br />
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**[[2wat]] - yACPS I PPT domain + CoA<br />
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*β-ketoacyl-ACPS II
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**[[1e5m]] - ACPS II – ''Synechocytosis''<br />
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**[[1j3n]] - TtACPS II – ''Thermus thermophilus''<br />
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**[[1ox0]], [[1oxh]] - SpACPS II<br />
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**[[2alm]], [[2rjt]] - MtACPS II (mutant)<br />
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**[[2gqd]] - SaACPS II <br />
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**[[2gp6]] - MtACPS II <br />
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**[[3e60]] – ACPS II – ''Bartonella henselae''<br />
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**[[3kzu]] - ACPS II – ''Brucella melitensis''<br />
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**[[3o04]], [[5sxo]] - ACPS II – ''Listeria monocytogenes''<br />
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**[[4ddo]] - BvACPS II – ''Burkholderia vietnamiensis''<br />
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**[[1kas]], [[2gfw]] – EcACPS II<br />
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**[[2gfv]] - EcACPS II (mutant)<br />
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**[[4b7v]] - PaACPS II – ''Pseudonomas aeruginosa''<br />
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**[[4jb6]] - PaACPS II (mutant)<br />
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**[[4jga]] - PaACPS II – ''Rickettsia rickettsii''<br />
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**[[4jrh]], [[4jrm]] - VcACPS II <br />
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**[[4ls5]] - BsACPS II <br />
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**[[4ls6]] - BsACPS II (mutant)<br />
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**[[4qav]], [[5cmo]] - NmACPS II – ''Nisseria meningitidis''<br />
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**[[4r8e]] - YpACPS II <br />
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*ACPS II complex
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**[[1b3n]] - EcACPS II + antibiotic<br />
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**[[2gfx]], [[3g0y]], [[3g11]], [[3hnz]], [[3ho2]], [[3ho9]], [[3i8p]] - EcACPS II (mutant) + antibiotic<br />
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**[[2gfy]] - EcACPS II (mutant) + dodecanoic acid<br />
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**[[4f32]] - BvACPS II + antibiotic<br />
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**[[4jpf]] - PaACPS II + inhibitor<br />
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**[[4ls7]], [[4ls8]] - BsACPS II + antibiotic<br />
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*β-ketoacyl-ACPS III
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**[[1hzp]], [[1m1m]] - MtACPS III <br />
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**[[1u6e]], [[2ahb]], [[2aj9]] - MtACPS III (mutant)<br />
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**[[1mzj]] - ACPS III – ''Streptomyces''<br />
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**[[1zow]], [[3il7]] - SaACPS III <br />
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**[[2ebd]] - ACPS III – ''Aquifex aeolicus''<br />
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**[[3gwa]], [[3gwe]] - ACPS III – ''Burkholderia pseudomallei''<br />
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**[[4dfe]], [[4efi]] - ACPS III – ''Burkholderia xenovorans''<br />
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**[[3il3]] - HiACPS III – ''Haemophilus influenza''<br />
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**[[3fk5]] - ACPS III – ''Xanthomonas oryzae''<br />
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**[[3led]] - ACPS III – ''Pseudonomas palustris''<br />
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**[[2x3e]] - PaACPS III <br />
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**[[5dwz]] - PaACPS III (mutant)<br />
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**[[1ebl]], [[1hn9]], [[1hnk]], [[3il9]] - EcACPS III<br />
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**[[4ewp]] – ACPS III – ''Micrococcus luteus''<br />
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**[[4ryb]] - NmACPS III <br />
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**[[4wzu]] - VcACPS III-2 <br />
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**[[4x9k]], [[4x9o]] - VcACPS III-2 (mutant)<br />
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**[[5by7]] - ACPS III – ''Verrucosispora maris''<br />
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**[[1ub7]] - TtACPS III (mutant)<br />
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**[[4z19]], [[4ylt]] - YpACPS III <br />
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*ACPS III complex
 
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**[[1hnd]], [[1hnh]], [[2gyo]], [[2eft]] - EcACPS III + CoA<br />
 
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**[[1hnj]] - EcACPS III + malonyl-CoA<br />
 
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**[[2qx1]] - EcACPS III + decyl-CoA<br />
 
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**[[1mzs]], [[5bnm]], [[5bnr]], [[5bns]] - EcACPS III + inhibitor<br />
 
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**[[5bqs]] - SpACPS III + inhibitor<br />
 
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**[[4z8d]] - HiACPS III + inhibitor<br />
 
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**[[1u6s]] - MtACPS III (mutant) + lauroyl-CoA<br />
 
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**[[2qnx]], [[2qo1]] - MtACPS III + undecanoic acid<br />
 
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**[[2qo0]] - MtACPS III (mutant) + undecanoic acid<br />
 
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**[[2qnz]] - MtACPS III + decyl formate<br />
 
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**[[2qny]] - MtACPS III (mutant) + decyl formate<br />
 
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**[[1ub7]] - TtACPS III (mutant)<br />
 
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**[[3il4]] - EfACPS III + CoA – ''Enterococcus faecalis''<br />
 
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**[[3il5]] - EfACPS III + benzoic acid derivative<br />
 
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**[[3il6]] - EfACPS III (mutant) + benzoic acid derivative<br />
 
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**[[4nhd]] - VcACPS III + CoA<br />
 
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**[[4x0o]] - VcACPS III-2 + acetyl-CoA<br />
 
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**[[5kp2]] - VcACPS III-2 + octanoyl-CoA<br />
 
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}}
 
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Acyl carrier protein synthase complex with CoA and Mg+2 ion (cyan) 3hqj

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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?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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