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3t57

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<StructureSection load='3t57' size='340' side='right'caption='[[3t57]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='3t57' size='340' side='right'caption='[[3t57]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3t57]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T57 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T57 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3t57]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T57 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T57 FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AT4g29540, lpxA, T16L4.50 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://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 [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.129 2.3.1.129] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3t57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t57 OCA], [https://pdbe.org/3t57 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t57 RCSB], [https://www.ebi.ac.uk/pdbsum/3t57 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t57 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=3t57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t57 OCA], [https://pdbe.org/3t57 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t57 RCSB], [https://www.ebi.ac.uk/pdbsum/3t57 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t57 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/LPXA_ARATH LPXA_ARATH]] Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that in bacteria anchors the lipopolysaccharide to the outer membrane of the cell. Lipid A-like molecules in plants may serve as structural components of the outer membranes of mitochondria and/or chloroplasts, or may be involved in signal transduction or plant defense responses (Potential).
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[https://www.uniprot.org/uniprot/LPXA_ARATH LPXA_ARATH] Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that in bacteria anchors the lipopolysaccharide to the outer membrane of the cell. Lipid A-like molecules in plants may serve as structural components of the outer membranes of mitochondria and/or chloroplasts, or may be involved in signal transduction or plant defense responses (Potential).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The UDP-N-acetylglucosamine (UDP-GlcNAc) acyltransferase, encoded by lpxA, catalyzes the first step of lipid A biosynthesis in Gram-negative bacteria, the (R)-3-hydroxyacyl-ACP-dependent acylation of the 3-OH group of UDP-GlcNAc. Recently, we demonstrated that the Arabidopsis thaliana orthologs of six enzymes of the bacterial lipid A pathway produce lipid A precursors with structures similar to those of Escherichia coli lipid A precursors [Li, C., et al. (2011) Proc. Natl. Acad. Sci. U.S.A. 108, 11387-11392]. To build upon this finding, we have cloned, purified, and determined the crystal structure of the A. thaliana LpxA ortholog (AtLpxA) to 2.1 A resolution. The overall structure of AtLpxA is very similar to that of E. coli LpxA (EcLpxA) with an alpha-helical-rich C-terminus and characteristic N-terminal left-handed parallel beta-helix (LbetaH). All key catalytic and chain length-determining residues of EcLpxA are conserved in AtLpxA; however, AtLpxA has an additional coil and loop added to the LbetaH not seen in EcLpxA. Consistent with the similarities between the two structures, purified AtLpxA catalyzes the same reaction as EcLpxA. In addition, A. thaliana lpxA complements an E. coli mutant lacking the chromosomal lpxA and promotes the synthesis of lipid A in vivo similar to the lipid A produced in the presence of E. coli lpxA. This work shows that AtLpxA is a functional UDP-GlcNAc acyltransferase that is able to catalyze the same reaction as EcLpxA and supports the hypothesis that lipid A molecules are biosynthesized in Arabidopsis and other plants.
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Activity and Crystal Structure of Arabidopsis thalianaUDP-N-Acetylglucosamine Acyltransferase.,Joo SH, Chung HS, Raetz CR, Garrett TA Biochemistry. 2012 May 14. PMID:22545860<ref>PMID:22545860</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3t57" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[UDP-N-acetylglucosamine acyltransferase|UDP-N-acetylglucosamine acyltransferase]]
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*[[UDP-N-acetylglucosamine acyltransferase 3D structures|UDP-N-acetylglucosamine acyltransferase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arath]]
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[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Joo, S H]]
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[[Category: Joo SH]]
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[[Category: Raetz, C R.H]]
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[[Category: Raetz CRH]]
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[[Category: Acylation]]
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[[Category: Acyltransferase]]
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[[Category: Left-handed parallel beta helix]]
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[[Category: Lipid a biosynthesis]]
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[[Category: Lipid synthesis]]
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[[Category: Transferase]]
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Current revision

Activity and Crystal Structure of Arabidopsis UDP-N-acetylglucosamine acyltransferase

PDB ID 3t57

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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