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| | ==Crystal structure of FabH from Micrococcus luteus== | | ==Crystal structure of FabH from Micrococcus luteus== |
| - | <StructureSection load='4ewp' size='340' side='right' caption='[[4ewp]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='4ewp' size='340' side='right'caption='[[4ewp]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ewp]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Miclc Miclc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EWP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EWP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ewp]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Micrococcus_luteus_NCTC_2665 Micrococcus luteus NCTC 2665]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EWP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EWP FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ebd|2ebd]]</td></tr> | + | </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=4ewp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ewp OCA], [https://pdbe.org/4ewp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ewp RCSB], [https://www.ebi.ac.uk/pdbsum/4ewp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ewp ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fabH, HMPREF0569_0014, Mlut_09310 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=465515 MICLC])</td></tr>
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| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-ketoacyl-[acyl-carrier-protein]_synthase_III Beta-ketoacyl-[acyl-carrier-protein] synthase III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.180 2.3.1.180] </span></td></tr>
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| - | <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=4ewp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ewp OCA], [http://pdbe.org/4ewp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ewp RCSB], [http://www.ebi.ac.uk/pdbsum/4ewp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ewp ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/C5CAR9_MICLC C5CAR9_MICLC]] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids (By similarity).[HAMAP-Rule:MF_01815] | + | [https://www.uniprot.org/uniprot/C5CAR9_MICLC C5CAR9_MICLC] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids (By similarity).[HAMAP-Rule:MF_01815] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Acyl carrier protein synthase|Acyl carrier protein synthase]] | + | *[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Miclc]] | + | [[Category: Large Structures]] |
| - | [[Category: Adams, P D]] | + | [[Category: Micrococcus luteus NCTC 2665]] |
| - | [[Category: Beller, H R]] | + | [[Category: Adams PD]] |
| - | [[Category: Goh, E B]] | + | [[Category: Beller HR]] |
| - | [[Category: Keasling, J D]] | + | [[Category: Goh E-B]] |
| - | [[Category: Pereira, J H]] | + | [[Category: Keasling JD]] |
| - | [[Category: Synthase]]
| + | [[Category: Pereira JH]] |
| - | [[Category: Transferase]]
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| Structural highlights
Function
C5CAR9_MICLC Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids (By similarity).[HAMAP-Rule:MF_01815]
Publication Abstract from PubMed
Micrococcus luteus is a Gram-positive bacterium that produces iso- and anteiso-branched alkenes by the head-to-head condensation of fatty-acid thioesters [coenzyme A (CoA) or acyl carrier protein (ACP)]; this activity is of interest for the production of advanced biofuels. In an effort to better understand the control of the formation of branched fatty acids in M. luteus, the structure of FabH (MlFabH) was determined. FabH, or beta-ketoacyl-ACP synthase III, catalyzes the initial step of fatty-acid biosynthesis: the condensation of malonyl-ACP with an acyl-CoA. Analysis of the MlFabH structure provides insights into its substrate selectivity with regard to length and branching of the acyl-CoA. The most structurally divergent region of FabH is the L9 loop region located at the dimer interface, which is involved in the formation of the acyl-binding channel and thus limits the substrate-channel size. The residue Phe336, which is positioned near the catalytic triad, appears to play a major role in branched-substrate selectivity. In addition to structural studies of MlFabH, transcriptional studies of M. luteus were also performed, focusing on the increase in the ratio of anteiso:iso-branched alkenes that was observed during the transition from early to late stationary phase. Gene-expression microarray analysis identified two genes involved in leucine and isoleucine metabolism that may explain this transition.
Structure of FabH and factors affecting the distribution of branched fatty acids in Micrococcus luteus.,Pereira JH, Goh EB, Keasling JD, Beller HR, Adams PD Acta Crystallogr D Biol Crystallogr. 2012 Oct;68(Pt 10):1320-8. Epub 2012 Sep 18. PMID:22993086[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Pereira JH, Goh EB, Keasling JD, Beller HR, Adams PD. Structure of FabH and factors affecting the distribution of branched fatty acids in Micrococcus luteus. Acta Crystallogr D Biol Crystallogr. 2012 Oct;68(Pt 10):1320-8. Epub 2012 Sep 18. PMID:22993086 doi:http://dx.doi.org/10.1107/S0907444912028351
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