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| | <StructureSection load='1zwj' size='340' side='right'caption='[[1zwj]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='1zwj' size='340' side='right'caption='[[1zwj]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1zwj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vkv 1vkv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZWJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZWJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1zwj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vkv 1vkv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZWJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZWJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2gdk|2gdk]], [[1z84|1z84]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At5g18200 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=1zwj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zwj OCA], [https://pdbe.org/1zwj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zwj RCSB], [https://www.ebi.ac.uk/pdbsum/1zwj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zwj 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=1zwj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zwj OCA], [https://pdbe.org/1zwj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zwj RCSB], [https://www.ebi.ac.uk/pdbsum/1zwj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zwj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/AGLUP_ARATH AGLUP_ARATH]] Catalyzes the conversion of ADP-glucose and inorganic phosphate (Pi) into glucose-1-phosphate and ADP. Does not possess galactose-1-phosphate uridylyltransferase activity.<ref>PMID:16519510</ref>
| + | [https://www.uniprot.org/uniprot/AGLUP_ARATH AGLUP_ARATH] Catalyzes the conversion of ADP-glucose and inorganic phosphate (Pi) into glucose-1-phosphate and ADP. Does not possess galactose-1-phosphate uridylyltransferase activity.<ref>PMID:16519510</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Allard, S T.M]] | + | [[Category: Allard STM]] |
| - | [[Category: Bingman, C A]] | + | [[Category: Bingman CA]] |
| - | [[Category: Bitto, E]] | + | [[Category: Bitto E]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Johnson KA]] |
| - | [[Category: Johnson, K A]] | + | [[Category: McCoy JG]] |
| - | [[Category: McCoy, J G]] | + | [[Category: Phillips Jr GN]] |
| - | [[Category: Phillips, G N]] | + | [[Category: Smith DW]] |
| - | [[Category: Smith, D W]] | + | [[Category: Wesenberg GE]] |
| - | [[Category: Wesenberg, G E]] | + | |
| - | [[Category: At5g18200]]
| + | |
| - | [[Category: Cesg]]
| + | |
| - | [[Category: Galt]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
AGLUP_ARATH Catalyzes the conversion of ADP-glucose and inorganic phosphate (Pi) into glucose-1-phosphate and ADP. Does not possess galactose-1-phosphate uridylyltransferase activity.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The X-ray crystal structure of the At5g18200.1 protein has been determined to a nominal resolution of 2.30 A. The structure has a histidine triad (HIT)-like fold containing two distinct HIT-like motifs. The sequence of At5g18200.1 indicates a distant family relationship to the Escherichia coli galactose-1-P uridylyltransferase (GalT): the determined structure of the At5g18200.1 protein confirms this relationship. The At5g18200.1 protein does not demonstrate GalT activity but instead catalyzes adenylyl transfer in the reaction of ADP-glucose with various phosphates. The best acceptor among those evaluated is phosphate itself; thus, the At5g18200.1 enzyme appears to be an ADP-glucose phosphorylase. The enzyme catalyzes the exchange of (14)C between ADP-[(14)C]glucose and glucose-1-P in the absence of phosphate. The steady state kinetics of exchange follows the ping-pong bi-bi kinetic mechanism, with a k(cat) of 4.1 s(-)(1) and K(m) values of 1.4 and 83 microM for ADP-[(14)C]glucose and glucose-1-P, respectively, at pH 8.5 and 25 degrees C. The overall reaction of ADP-glucose with phosphate to produce ADP and glucose-1-P follows ping-pong bi-bi steady state kinetics, with a k(cat) of 2.7 s(-)(1) and K(m) values of 6.9 and 90 microM for ADP-glucose and phosphate, respectively, at pH 8.5 and 25 degrees C. The kinetics are consistent with a double-displacement mechanism that involves a covalent adenylyl-enzyme intermediate. The X-ray crystal structure of this intermediate was determined to 1.83 A resolution and shows the AMP group bonded to His(186). The value of K(eq) in the direction of ADP and glucose-1-P formation is 5.0 at pH 7.0 and 25 degrees C in the absence of a divalent metal ion, and it is 40 in the presence of 1 mM MgCl(2).
Structure and mechanism of an ADP-glucose phosphorylase from Arabidopsis thaliana.,McCoy JG, Arabshahi A, Bitto E, Bingman CA, Ruzicka FJ, Frey PA, Phillips GN Jr Biochemistry. 2006 Mar 14;45(10):3154-62. PMID:16519510[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ McCoy JG, Arabshahi A, Bitto E, Bingman CA, Ruzicka FJ, Frey PA, Phillips GN Jr. Structure and mechanism of an ADP-glucose phosphorylase from Arabidopsis thaliana. Biochemistry. 2006 Mar 14;45(10):3154-62. PMID:16519510 doi:10.1021/bi052232m
- ↑ McCoy JG, Arabshahi A, Bitto E, Bingman CA, Ruzicka FJ, Frey PA, Phillips GN Jr. Structure and mechanism of an ADP-glucose phosphorylase from Arabidopsis thaliana. Biochemistry. 2006 Mar 14;45(10):3154-62. PMID:16519510 doi:10.1021/bi052232m
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