|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Activity and Crystal Structure of Francisella novicida UDP-N-Acetylglucosamine Acyltransferase== | | ==Activity and Crystal Structure of Francisella novicida UDP-N-Acetylglucosamine Acyltransferase== |
| - | <StructureSection load='5f42' size='340' side='right' caption='[[5f42]], [[Resolution|resolution]] 2.06Å' scene=''> | + | <StructureSection load='5f42' size='340' side='right'caption='[[5f42]], [[Resolution|resolution]] 2.06Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5f42]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F42 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F42 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5f42]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Francisella_tularensis_subsp._novicida_U112 Francisella tularensis subsp. novicida U112]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F42 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F42 FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine_O-acyltransferase Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.129 2.3.1.129] </span></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]] 2.06Å</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=5f42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f42 OCA], [http://pdbe.org/5f42 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f42 RCSB], [http://www.ebi.ac.uk/pdbsum/5f42 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f42 ProSAT]</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=5f42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f42 OCA], [https://pdbe.org/5f42 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f42 RCSB], [https://www.ebi.ac.uk/pdbsum/5f42 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f42 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0Q7Y0_FRATN A0Q7Y0_FRATN]] Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.[SAAS:SAAS00001305] | + | [https://www.uniprot.org/uniprot/A0Q7Y0_FRATN A0Q7Y0_FRATN] Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.[SAAS:SAAS00001305] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 18: |
Line 18: |
| | </div> | | </div> |
| | <div class="pdbe-citations 5f42" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5f42" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[UDP-N-acetylglucosamine acyltransferase|UDP-N-acetylglucosamine acyltransferase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Joo, S H]] | + | [[Category: Francisella tularensis subsp. novicida U112]] |
| - | [[Category: Raetz, C R.H]] | + | [[Category: Large Structures]] |
| - | [[Category: Left-handed parallel beta helix]] | + | [[Category: Joo SH]] |
| - | [[Category: Transferase]] | + | [[Category: Raetz CRH]] |
| Structural highlights
Function
A0Q7Y0_FRATN Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.[SAAS:SAAS00001305]
Publication Abstract from PubMed
The first step of lipid A biosynthesis in Escherichia coli (E. coli) is catalyzed by LpxA (EcLpxA), an acyltransferase selective for UDP-N-acetylglucosamine (UDP-GlcNAc) and R-3-hydroxymyristoyl-acyl carrier protein (3-OH-C14-ACP), and is an essential step in majority of Gram-negative bacteria. Since the majority of lipid A species isolated from F. novicida contains 3-OH-C16 or 3-OH-C18 at its C3 and C3' positions, FnLpxA was thought to be selective for longer acyl chain (3-OH-C16 and 3-OH-C18) over short acyl chain (3-OH-C14, 3-OH-C12, and 3-OH-C10). Here we demonstrate that Francisella novicida (F. novicida) lpxA functionally complements an E. coli lpxA knockout mutant and efficiently transfers 3-OH-C14 as well as 3-OH-C16 in E. coli. Our results implicate that the acyl chain length of lipid A is determined by several factors including acyl chain selectivity of LpxA and downstream enzymes, as well as the composition of the acyl-ACP pool in vivo. We also report the crystal structure of F. novicida LpxA (FnLpxA) at 2.06 A. The N-terminal parallel beta-helix (LbetaH) and C-terminal alpha-helical domain are similar to other reported structures of LpxAs. However, our structure indicates that the supposed ruler residues for hydrocarbon length, 171L in one monomer and 168H in the adjacent monomer in a functional trimer of FnLpxA, are located just 3.8 A apart that renders not enough space for binding of 3-OH-C12 or longer acyl chains. This implicates that FnLpxA may have an alternative hydrophobic pocket, or the acyl chain may bend while binding to FnLpxA. In addition, the FnLpxA structure suggests a potential inhibitor binding site for development of antibiotics.
Crystal structure and activity of Francisella novicida UDP-N-acetylglucosamine acyltransferase.,Joo SH, Chung HS Biochem Biophys Res Commun. 2016 Sep 23;478(3):1223-9. doi:, 10.1016/j.bbrc.2016.08.098. Epub 2016 Aug 19. PMID:27545601[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Joo SH, Chung HS. Crystal structure and activity of Francisella novicida UDP-N-acetylglucosamine acyltransferase. Biochem Biophys Res Commun. 2016 Sep 23;478(3):1223-9. doi:, 10.1016/j.bbrc.2016.08.098. Epub 2016 Aug 19. PMID:27545601 doi:http://dx.doi.org/10.1016/j.bbrc.2016.08.098
|
