5j63: Difference between revisions

Latest revision as of 10:50, 6 September 2023

Crystal Structure of the N-terminal N-formyltransferase Domain (residues 1-306) of Escherichia coli Arna in Complex with UDP-Ara4N and Folinic Acid

Structural highlights

5j63 is a 4 chain structure with sequence from Escherichia coli H736. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Ligands:	FNX, G3N
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

ArnA from Escherichia coli is a key enzyme involved in the formation of 4-amino-4-deoxy-l-arabinose. The addition of this sugar to the lipid A moiety of the lipopolysaccharide of pathogenic Gram-negative bacteria allows these organisms to evade the cationic antimicrobial peptides of the host immune system. Indeed, it is thought that such modifications may be responsible for the repeated infections of cystic fibrosis patients with Pseudomonas aeruginosa. ArnA is a bifunctional enzyme with the N- and C-terminal domains catalyzing formylation and oxidative decarboxylation reactions, respectively. The catalytically competent cofactor for the formylation reaction is N10 -formyltetrahydrofolate. Here we describe the structure of the isolated N-terminal domain of ArnA in complex with its UDP-sugar substrate and N5 -formyltetrahydrofolate. The model presented herein may prove valuable in the development of new antimicrobial therapeutics. This article is protected by copyright. All rights reserved.

Structure of the Escherichia coli ArnA N-Formyltransferase Domain in Complex with N -formyltetrahydrofolate and UDP-Ara4N.,Genthe NA, Thoden JB, Holden HM Protein Sci. 2016 May 12. doi: 10.1002/pro.2938. PMID:27171345^[1]

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

References

↑ Genthe NA, Thoden JB, Holden HM. Structure of the Escherichia coli ArnA N-Formyltransferase Domain in Complex with N -formyltetrahydrofolate and UDP-Ara4N. Protein Sci. 2016 May 12. doi: 10.1002/pro.2938. PMID:27171345 doi:https://dx.doi.org/10.1002/pro.2938

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OCA

[1] Genthe NA, Thoden JB, Holden HM. Structure of the Escherichia coli ArnA N-Formyltransferase Domain in Complex with N -formyltetrahydrofolate and UDP-Ara4N. Protein Sci. 2016 May 12. doi: 10.1002/pro.2938. PMID:27171345 doi:https://dx.doi.org/10.1002/pro.2938

[1]

@@ Line 3: / Line 3: @@
 <StructureSection load='5j63' size='340' side='right'caption='[[5j63]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5j63]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_h736 Escherichia coli h736]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J63 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J63 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5j63]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_H736 Escherichia coli H736]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J63 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5J63 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FNX:(4AS,6S)-2-AMINO-6-{(E)-[(4-METHYLPHENYL)IMINO]METHYL}-4-OXO-4,6,7,8-TETRAHYDROPTERIDINE-5(4AH)-CARBALDEHYDE'>FNX</scene>, <scene name='pdbligand=G3N:(2R,3R,4S,5S)-5-AMINO-3,4-DIHYDROXYTETRAHYDRO-2H-PYRAN-2-YL+[(2R,3S,4R,5R)-5-(2,4-DIOXO-3,4-DIHYDROPYRIMIDIN-1(2H)-YL)-3,4-DIHYDROXYTETRAHYDROFURAN-2-YL]METHYL+DIHYDROGEN+DIPHOSPHATE'>G3N</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]] 2.5&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">arnA, ECHG_02161 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=656414 Escherichia coli H736])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FNX:(4AS,6S)-2-AMINO-6-{(E)-[(4-METHYLPHENYL)IMINO]METHYL}-4-OXO-4,6,7,8-TETRAHYDROPTERIDINE-5(4AH)-CARBALDEHYDE'>FNX</scene>, <scene name='pdbligand=G3N:(2R,3R,4S,5S)-5-AMINO-3,4-DIHYDROXYTETRAHYDRO-2H-PYRAN-2-YL+[(2R,3S,4R,5R)-5-(2,4-DIOXO-3,4-DIHYDROPYRIMIDIN-1(2H)-YL)-3,4-DIHYDROXYTETRAHYDROFURAN-2-YL]METHYL+DIHYDROGEN+DIPHOSPHATE'>G3N</scene></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=5j63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j63 OCA], [http://pdbe.org/5j63 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j63 RCSB], [http://www.ebi.ac.uk/pdbsum/5j63 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j63 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=5j63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j63 OCA], [https://pdbe.org/5j63 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5j63 RCSB], [https://www.ebi.ac.uk/pdbsum/5j63 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5j63 ProSAT]</span></td></tr>
 </table>
-== Function ==
-[[http://www.uniprot.org/uniprot/F4SGI5_ECOLX F4SGI5_ECOLX]] Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.[HAMAP-Rule:MF_01166][SAAS:SAAS00331614]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 21: @@
 __TOC__
 </StructureSection>
-[[Category: Escherichia coli h736]]
+[[Category: Escherichia coli H736]]
 [[Category: Large Structures]]
-[[Category: Genthe, N A]]
+[[Category: Genthe NA]]
-[[Category: Holden, H M]]
+[[Category: Holden HM]]
-[[Category: Thoden, J B]]
+[[Category: Thoden JB]]
-[[Category: Lipopolysaccharide]]
-[[Category: Transferase]]

5j63: Difference between revisions

Latest revision as of 10:50, 6 September 2023

Crystal Structure of the N-terminal N-formyltransferase Domain (residues 1-306) of Escherichia coli Arna in Complex with UDP-Ara4N and Folinic Acid

Structural highlights

Publication Abstract from PubMed

References

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