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2h39

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[[Image:2h39.gif|left|200px]]
 
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{{Structure
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==Crystal Structure of an ADP-Glucose Phosphorylase from Arabidopsis thaliana with bound ADP-Glucose==
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|PDB= 2h39 |SIZE=350|CAPTION= <scene name='initialview01'>2h39</scene>, resolution 2.230&Aring;
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<StructureSection load='2h39' size='340' side='right'caption='[[2h39]], [[Resolution|resolution]] 2.23&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=ADQ:ADENOSINE-5'-DIPHOSPHATE-GLUCOSE'>ADQ</scene>
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<table><tr><td colspan='2'>[[2h39]] 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=2gdk 2gdk]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H39 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H39 FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/UDP-glucose--hexose-1-phosphate_uridylyltransferase UDP-glucose--hexose-1-phosphate uridylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.12 2.7.7.12]
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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]] 2.23&#8491;</td></tr>
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|GENE= At5g18200 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADQ:ADENOSINE-5-DIPHOSPHATE-GLUCOSE'>ADQ</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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}}
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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=2h39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h39 OCA], [https://pdbe.org/2h39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h39 RCSB], [https://www.ebi.ac.uk/pdbsum/2h39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h39 ProSAT]</span></td></tr>
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</table>
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'''Crystal Structure of an ADP-Glucose Phosphorylase from Arabidopsis thaliana with bound ADP-Glucose'''
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== Function ==
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[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>
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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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).
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h3/2h39_consurf.spt"</scriptWhenChecked>
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2H39 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. This structure supersedes the now removed PDB entry 2GDK. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H39 OCA].
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==Reference==
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</jmolCheckbox>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16519510 16519510]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2h39 ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: UDP-glucose--hexose-1-phosphate uridylyltransferase]]
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[[Category: Bingman CA]]
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[[Category: Bingman, C A.]]
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[[Category: Bitto E]]
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[[Category: Bitto, E.]]
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[[Category: McCoy JG]]
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[[Category: CESG, Center for Eukaryotic Structural Genomics.]]
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[[Category: Phillips Jr GN]]
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[[Category: Jr., G N.Phillips.]]
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[[Category: Wesenberg GE]]
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[[Category: McCoy, J G.]]
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[[Category: Wesenberg, G E.]]
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[[Category: ADQ]]
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[[Category: CL]]
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[[Category: ZN]]
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[[Category: adp-glucose]]
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[[Category: at5g18200]]
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[[Category: center for eukaryotic structural genomic]]
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[[Category: cesg]]
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[[Category: galt-like]]
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[[Category: protein structure initiative]]
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[[Category: psi]]
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[[Category: structural genomics functional follow-up study]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:12:08 2008''
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Current revision

Crystal Structure of an ADP-Glucose Phosphorylase from Arabidopsis thaliana with bound ADP-Glucose

PDB ID 2h39

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