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4nbt

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Revision as of 07:30, 23 December 2016

Crystal structure of FabG from Acholeplasma laidlawii

Structural highlights

4nbt is a 4 chain structure with sequence from Achli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1q7b, 4nbu, 4nbv, 4nbw
Gene:	fabG2, ACL_0504 (ACHLI)
Activity:	[acyl-carrier-protein_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number 1.1.1.100
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Major efforts in bioenergy research have focused on producing fuels that can directly replace petroleum-derived gasoline and diesel fuel through metabolic engineering of microbial fatty acid biosynthetic pathways. Typically, growth and pathway induction are conducted under aerobic conditions, but for operational efficiency in an industrial context, anaerobic culture conditions would be preferred to obviate the need to maintain specific dissolved oxygen concentrations and to maximize the proportion of reducing equivalents directed to biofuel biosynthesis rather than ATP production. A major concern with fermentative growth conditions is elevated NADH levels, which can adversely affect cell physiology. The purpose of this study was to identify homologs of Escherichia coli FabG, an essential reductase involved in fatty acid biosynthesis, that display a higher preference for NADH than for NADPH as a cofactor. Four potential NADH-dependent FabG variants were identified through bioinformatic analyses supported by crystallographic structure determination (1.3 to 2.0 A-resolution). In vitro assays of cofactor (NADH/NADPH) preference in the four variants showed up to approximately 35-fold preference for NADH, which was observed with the Cupriavidus taiwanensis FabG variant. In addition, FabG homologs were overexpressed in fatty acid- and methyl ketone-overproducing E. coli host strains under anaerobic conditions, and the C. taiwanensis variant led to a 60% higher free fatty acid titer and 75% higher methyl ketone titer relative to the control strains. With further engineering, this work could serve as a starting point for establishing a microbial host strain for production of fatty acid-derived biofuels (e.g., methyl ketones) under anaerobic conditions.

Biochemical and Structural Studies of NADH-Dependent FabG Used to Increase the Bacterial Production of Fatty Acids under Anaerobic Conditions.,Javidpour P, Pereira JH, Goh EB, McAndrew RP, Ma SM, Friedland GD, Keasling JD, Chhabra SR, Adams PD, Beller HR Appl Environ Microbiol. 2013 Nov 8. PMID:24212572^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Javidpour P, Pereira JH, Goh EB, McAndrew RP, Ma SM, Friedland GD, Keasling JD, Chhabra SR, Adams PD, Beller HR. Biochemical and Structural Studies of NADH-Dependent FabG Used to Increase the Bacterial Production of Fatty Acids under Anaerobic Conditions. Appl Environ Microbiol. 2013 Nov 8. PMID:24212572 doi:http://dx.doi.org/10.1128/AEM.03194-13

1 Structural highlights
2 Publication Abstract from PubMed
3 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4nbt"

@@ Line 1: / Line 1: @@
 ==Crystal structure of FabG from Acholeplasma laidlawii==
 <StructureSection load='4nbt' size='340' side='right' caption='[[4nbt]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fabG2, ACL_0504 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=441768 ACHLI])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-oxoacyl-[acyl-carrier-protein]_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.100 1.1.1.100] </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=4nbt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nbt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nbt RCSB], [http://www.ebi.ac.uk/pdbsum/4nbt PDBsum]</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=4nbt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nbt OCA], [http://pdbe.org/4nbt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nbt RCSB], [http://www.ebi.ac.uk/pdbsum/4nbt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nbt ProSAT]</span></td></tr>
 </table>
 <div style="background-color:#fffaf0;">
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4nbt" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4nbt

From Proteopedia

Revision as of 07:30, 23 December 2016

Crystal structure of FabG from Acholeplasma laidlawii

Structural highlights

Publication Abstract from PubMed

References

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