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| | <StructureSection load='6n3p' size='340' side='right'caption='[[6n3p]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='6n3p' size='340' side='right'caption='[[6n3p]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6n3p]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N3P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6N3P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6n3p]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N3P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6N3P FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=XLN:N~3~-{(2R)-4-[(dihydroxyphosphanyl)oxy]-2-hydroxy-3,3-dimethylbutanoyl}-N-(3-{[(1Z)-pent-1-en-1-yl]sulfonyl}propyl)-beta-alaninamide'>XLN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fabZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), acpP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=XLN:N~3~-{(2R)-4-[(dihydroxyphosphanyl)oxy]-2-hydroxy-3,3-dimethylbutanoyl}-N-(3-{[(1Z)-pent-1-en-1-yl]sulfonyl}propyl)-beta-alaninamide'>XLN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-hydroxyacyl-[acyl-carrier-protein]_dehydratase 3-hydroxyacyl-[acyl-carrier-protein] dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.59 4.2.1.59] </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=6n3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n3p OCA], [https://pdbe.org/6n3p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6n3p RCSB], [https://www.ebi.ac.uk/pdbsum/6n3p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6n3p ProSAT]</span></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=6n3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n3p OCA], [http://pdbe.org/6n3p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6n3p RCSB], [http://www.ebi.ac.uk/pdbsum/6n3p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6n3p ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FABZ_ECO45 FABZ_ECO45]] Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. [[http://www.uniprot.org/uniprot/ACP_ECO45 ACP_ECO45]] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[HAMAP-Rule:MF_01217] | + | [https://www.uniprot.org/uniprot/FABZ_ECOLI FABZ_ECOLI] Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.<ref>PMID:10629181</ref> <ref>PMID:7806516</ref> <ref>PMID:8910376</ref> |
| | <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 3D structures|Acyl carrier protein 3D structures]] |
| | *[[Beta-hydroxyacyl-acyl carrier protein dehydratase 3D structures|Beta-hydroxyacyl-acyl carrier protein dehydratase 3D structures]] | | *[[Beta-hydroxyacyl-acyl carrier protein dehydratase 3D structures|Beta-hydroxyacyl-acyl carrier protein dehydratase 3D structures]] |
| | == References == | | == References == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dodge, G J]] | + | [[Category: Dodge GJ]] |
| - | [[Category: Smith, J L]] | + | [[Category: Smith JL]] |
| - | [[Category: Acp]]
| + | |
| - | [[Category: Acpp]]
| + | |
| - | [[Category: Acyl carrier protein]]
| + | |
| - | [[Category: Biosynthetic protein]]
| + | |
| - | [[Category: Crosslinking]]
| + | |
| - | [[Category: Dehydratase]]
| + | |
| - | [[Category: E. coli]]
| + | |
| - | [[Category: Fa]]
| + | |
| - | [[Category: Fabz]]
| + | |
| - | [[Category: Fatty acid biosynthsis]]
| + | |
| Structural highlights
Function
FABZ_ECOLI Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.[1] [2] [3]
Publication Abstract from PubMed
Fatty acid biosynthesis in alpha- and gamma-proteobacteria requires two functionally distinct dehydratases, FabA and FabZ. Here, mechanistic cross-linking facilitates the structural characterization of a stable hexameric complex of six Escherichia coli FabZ dehydratase subunits with six AcpP acyl carrier proteins. The crystal structure sheds light on the divergent substrate selectivity of FabA and FabZ by revealing distinct architectures of the binding pocket. Molecular dynamics simulations demonstrate differential biasing of substrate orientations and conformations within the active sites of FabA and FabZ such that FabZ is preorganized to catalyze only dehydration, while FabA is primed for both dehydration and isomerization.
Structural and dynamical rationale for fatty acid unsaturation in Escherichia coli.,Dodge GJ, Patel A, Jaremko KL, McCammon JA, Smith JL, Burkart MD Proc Natl Acad Sci U S A. 2019 Mar 14. pii: 1818686116. doi:, 10.1073/pnas.1818686116. PMID:30872475[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Choi KH, Heath RJ, Rock CO. beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis. J Bacteriol. 2000 Jan;182(2):365-70. PMID:10629181 doi:10.1128/JB.182.2.365-370.2000
- ↑ Mohan S, Kelly TM, Eveland SS, Raetz CR, Anderson MS. An Escherichia coli gene (FabZ) encoding (3R)-hydroxymyristoyl acyl carrier protein dehydrase. Relation to fabA and suppression of mutations in lipid A biosynthesis. J Biol Chem. 1994 Dec 30;269(52):32896-903 PMID:7806516
- ↑ Heath RJ, Rock CO. Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis. J Biol Chem. 1996 Nov 1;271(44):27795-801. PMID:8910376
- ↑ Dodge GJ, Patel A, Jaremko KL, McCammon JA, Smith JL, Burkart MD. Structural and dynamical rationale for fatty acid unsaturation in Escherichia coli. Proc Natl Acad Sci U S A. 2019 Mar 14. pii: 1818686116. doi:, 10.1073/pnas.1818686116. PMID:30872475 doi:http://dx.doi.org/10.1073/pnas.1818686116
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