1yp4
From Proteopedia
(Difference between revisions)
(9 intermediate revisions not shown.) | |||
Line 1: | Line 1: | ||
- | [[Image:1yp4.png|left|200px]] | ||
- | + | ==Crystal structure of potato tuber ADP-glucose pyrophosphorylase in complex with ADP-glucose== | |
+ | <StructureSection load='1yp4' size='340' side='right'caption='[[1yp4]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[1yp4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Solanum_tuberosum Solanum tuberosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YP4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YP4 FirstGlance]. <br> | ||
+ | </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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ADQ:ADENOSINE-5-DIPHOSPHATE-GLUCOSE'>ADQ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1yp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yp4 OCA], [https://pdbe.org/1yp4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yp4 RCSB], [https://www.ebi.ac.uk/pdbsum/1yp4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yp4 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/GLGS_SOLTU GLGS_SOLTU] This protein plays a role in synthesis of starch. It catalyzes the synthesis of the activated glycosyl donor, ADP-glucose from Glc-1-P and ATP. | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yp/1yp4_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </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=1yp4 ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | ADP-glucose pyrophosphorylase catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria, being allosterically activated or inhibited by metabolites of energy flux. We report the first atomic resolution structure of ADP-glucose pyrophosphorylase. Crystals of potato tuber ADP-glucose pyrophosphorylase alpha subunit were grown in high concentrations of sulfate, resulting in the sulfate-bound, allosterically inhibited form of the enzyme. The N-terminal catalytic domain resembles a dinucleotide-binding Rossmann fold and the C-terminal domain adopts a left-handed parallel beta helix that is involved in cooperative allosteric regulation and a unique oligomerization. We also report structures of the enzyme in complex with ATP and ADP-glucose. Communication between the regulator-binding sites and the active site is both subtle and complex and involves several distinct regions of the enzyme including the N-terminus, the glucose-1-phosphate-binding site, and the ATP-binding site. These structures provide insights into the mechanism for catalysis and allosteric regulation of the enzyme. | ||
- | + | Crystal structure of potato tuber ADP-glucose pyrophosphorylase.,Jin X, Ballicora MA, Preiss J, Geiger JH EMBO J. 2005 Feb 23;24(4):694-704. Epub 2005 Feb 3. PMID:15692569<ref>PMID:15692569</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 1yp4" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | + | <references/> | |
- | == | + | __TOC__ |
- | < | + | </StructureSection> |
- | [[Category: | + | [[Category: Large Structures]] |
[[Category: Solanum tuberosum]] | [[Category: Solanum tuberosum]] | ||
- | [[Category: Ballicora | + | [[Category: Ballicora MA]] |
- | [[Category: Geiger | + | [[Category: Geiger JH]] |
- | [[Category: Jin | + | [[Category: Jin X]] |
- | [[Category: Preiss | + | [[Category: Preiss J]] |
- | + | ||
- | + |
Current revision
Crystal structure of potato tuber ADP-glucose pyrophosphorylase in complex with ADP-glucose
|