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| | <StructureSection load='5mni' size='340' side='right'caption='[[5mni]], [[Resolution|resolution]] 3.09Å' scene=''> | | <StructureSection load='5mni' size='340' side='right'caption='[[5mni]], [[Resolution|resolution]] 3.09Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5mni]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MNI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5MNI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5mni]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MNI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MNI FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glgC, b3430, JW3393 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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]] 3.09Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-1-phosphate_adenylyltransferase Glucose-1-phosphate adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.27 2.7.7.27] </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=5mni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mni OCA], [https://pdbe.org/5mni PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mni RCSB], [https://www.ebi.ac.uk/pdbsum/5mni PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mni ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5mni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mni OCA], [http://pdbe.org/5mni PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mni RCSB], [http://www.ebi.ac.uk/pdbsum/5mni PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mni ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GLGC_ECOLI GLGC_ECOLI]] Catalyzes the synthesis of ADP-glucose, a sugar donor used in elongation reactions on alpha-glucans. | + | [https://www.uniprot.org/uniprot/GLGC_ECOLI GLGC_ECOLI] Catalyzes the synthesis of ADP-glucose, a sugar donor used in elongation reactions on alpha-glucans. |
| | <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: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Glucose-1-phosphate adenylyltransferase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cifuente, J O]] | + | [[Category: Cifuente JO]] |
| - | [[Category: Comino, N]] | + | [[Category: Comino N]] |
| - | [[Category: Eguskiza, A]] | + | [[Category: Eguskiza A]] |
| - | [[Category: Guerin, M E]] | + | [[Category: Guerin ME]] |
| - | [[Category: Marina, A]] | + | [[Category: Marina A]] |
| - | [[Category: Orrantia, A]] | + | [[Category: Orrantia A]] |
| - | [[Category: Ec. 2 7.7 27 glycogen biosynthesis adp-glucose pyrophosphorilase nucleotidyltransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
GLGC_ECOLI Catalyzes the synthesis of ADP-glucose, a sugar donor used in elongation reactions on alpha-glucans.
Publication Abstract from PubMed
ADP-glucose pyrophosphorylase (AGPase) controls bacterial glycogen and plant starch biosynthetic pathways, the most common carbon storage polysaccharides in nature. AGPase activity is allosterically regulated by a series of metabolites in the energetic flux within the cell. Very recently, we reported the first crystal structures of the paradigmatic AGPase from Escherichia coli (EcAGPase) in complex with its preferred physiological negative and positive allosteric regulators, adenosine-5'-monophosphate (AMP) and fructose-1,6-bisphosphate (FBP), respectively. However, the understanding of the molecular mechanism by which AMP and FBP allosterically modulates EcAGPase enzymatic activity still remains enigmatic. Here we found that single point mutations of key residues in the AMP binding site decrease its inhibitory effect, but also clearly abolish the overall AMP-mediated stabilization effect in wild-type EcAGPase. Single point mutations of key residues for FBP binding did not revert the AMP-mediated stabilization. Strikingly, an EcAGPase.Arg130Ala mutant displayed a dramatic increase in the activity when compared with wild-type EcAGPase, and this increase correlated with a significant increment of glycogen content in vivo. The crystal structure of EcAGPase.Arg130Ala revealed unprecedented conformational changes in structural elements involved in the allosteric signal transmission. Altogether, we propose a model in which the positive and negative energy reporters regulate AGPase catalytic activity via intra- and inter-protomer crosstalk, with a 'sensory motif' and two loops RL1 and RL2 flanking the ATP binding site playing a significant role. The information reported herein provides exciting possibilities for industrial/biotechnological applications.
Mechanistic insights into the allosteric regulation of bacterial ADP-glucose pyrophosphorylases.,Comino N, Cifuente J, Marina A, Orrantia A, Eguskiza A, Guerin ME J Biol Chem. 2017 Feb 21. pii: jbc.M116.773408. doi: 10.1074/jbc.M116.773408. PMID:28223362[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Comino N, Cifuente J, Marina A, Orrantia A, Eguskiza A, Guerin ME. Mechanistic insights into the allosteric regulation of bacterial ADP-glucose pyrophosphorylases. J Biol Chem. 2017 Feb 21. pii: jbc.M116.773408. doi: 10.1074/jbc.M116.773408. PMID:28223362 doi:http://dx.doi.org/10.1074/jbc.M116.773408
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