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| | <StructureSection load='6bwc' size='340' side='right'caption='[[6bwc]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='6bwc' size='340' side='right'caption='[[6bwc]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6bwc]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_thuringiensis_hd-771 Bacillus thuringiensis hd-771]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BWC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BWC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6bwc]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis_HD-771 Bacillus thuringiensis HD-771]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BWC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</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]] 2.7Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BTG_02000 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1218175 Bacillus thuringiensis HD-771])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</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=6bwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bwc OCA], [http://pdbe.org/6bwc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bwc RCSB], [http://www.ebi.ac.uk/pdbsum/6bwc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bwc 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=6bwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bwc OCA], [https://pdbe.org/6bwc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bwc RCSB], [https://www.ebi.ac.uk/pdbsum/6bwc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bwc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/J3UJH9_BACTU J3UJH9_BACTU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus thuringiensis hd-771]] | + | [[Category: Bacillus thuringiensis HD-771]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Delvaux, N A]] | + | [[Category: Delvaux NA]] |
| - | [[Category: Holden, H M]] | + | [[Category: Holden HM]] |
| - | [[Category: Thoden, J B]] | + | [[Category: Thoden JB]] |
| - | [[Category: Biosynthetic protein]]
| + | |
| - | [[Category: Deoxy-sugar]]
| + | |
| - | [[Category: Flagellin glycosylation]]
| + | |
| - | [[Category: Shout chain dehydrogenase]]
| + | |
| Structural highlights
Function
J3UJH9_BACTU
Publication Abstract from PubMed
Bacillus thuringiensis is a soil-dwelling Gram positive bacterium that has been utilized as a biopesticide for well over 60 years. It is known to contain flagella that are important for motility. One of the proteins found in flagella is flagellin, which is post-translationally modified by O-glycosylation with derivatives of pseudaminic acid. The biosynthetic pathway for the production of CMP-pseudaminic acid in B. thuringiensis, starting with UDP-N-acetyl-d-glucosamine (UDP-GlcNAc), requires seven enzymes. Here we report the three-dimensional structures of Pen and Pal, which catalyze the first and second steps, respectively. Pen contains a tightly bound NADP(H) cofactor whereas Pal is isolated with bound NAD(H). For the X-ray analysis of Pen, the site-directed D128N/K129A mutant variant was prepared in order to trap its substrate, UDP-GlcNAc, into the active site. Pen adopts a hexameric quaternary structure with each subunit showing the bilobal architecture observed for members of the short-chain dehydrogenase/reductase superfamily. The hexameric quaternary structure is atypical for most members of the superfamily. The structure of Pal was determined in the presence of UDP. Pen adopts the more typical dimeric quaternary structure. Taken together, Pen and Pal catalyze the conversion of UDP-GlcNAc to UDP-4-keto-6-deoxy-l-N-acetylaltrosamine. Strikingly, in Gram negative bacteria such as Campylobacter jejuni and Helicobacter pylori, only a single enzyme (FlaA1) is required for the production of UDP-4-keto-6-deoxy-l-N-acetylaltrosamine. A comparison of Pen and Pal with FlaA1 reveals differences that may explain why FlaA1 is a bifunctional enzyme whereas Pen and Pal catalyze the individual steps leading to the formation of the UDP-sugar product. This investigation represents the first structural analysis of the enzymes in B. thuringiensis that are required for CMP-pseudaminic acid formation. This article is protected by copyright. All rights reserved.
Molecular Architectures of Pen and Pal: Key Enzymes Required for CMP-Pseudaminic Acid Biosynthesis in Bacillus thuringiensis.,Delvaux NA, Thoden JB, Holden HM Protein Sci. 2017 Dec 20. doi: 10.1002/pro.3368. PMID:29266550[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Delvaux NA, Thoden JB, Holden HM. Molecular Architectures of Pen and Pal: Key Enzymes Required for CMP-Pseudaminic Acid Biosynthesis in Bacillus thuringiensis. Protein Sci. 2017 Dec 20. doi: 10.1002/pro.3368. PMID:29266550 doi:http://dx.doi.org/10.1002/pro.3368
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