5lu4
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==C4-type pyruvate phosphate dikinase: conformational intermediate of central domain in the swiveling mechanism== | |
| + | <StructureSection load='5lu4' size='340' side='right' caption='[[5lu4]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5lu4]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LU4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LU4 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate,_phosphate_dikinase Pyruvate, phosphate dikinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.9.1 2.7.9.1] </span></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=5lu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lu4 OCA], [http://pdbe.org/5lu4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lu4 RCSB], [http://www.ebi.ac.uk/pdbsum/5lu4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lu4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PPDK_FLATR PPDK_FLATR]] Formation of phosphoenolpyruvate, which is the primary acceptor of CO(2) in C4 and some Crassulacean acid metabolism plants. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Pyruvate phosphate dikinase (PPDK) is an essential enzyme of both the C4 photosynthetic pathway and cellular energy metabolism of some bacteria and unicellular protists. In C4 plants, it catalyzes the ATP- and Pi -dependent formation of phosphoenolpyruvate (PEP) while in bacteria and protozoa the ATP-forming direction is used. PPDK is composed out of three distinct domains and exhibits one of the largest single domain movements known today during its catalytic cycle. However, little information about potential intermediate steps of this movement was available. A recent study resolved a discrete intermediate step of PPDK's swiveling movement, shedding light on the details of this intriguing mechanism. Here we present an additional structural intermediate that possibly represents another crucial step in the catalytic cycle of PPDK, providing means to get a more detailed understanding of PPDK's mode of function. | ||
| - | + | Trapped intermediate state of plant pyruvate phosphate dikinase indicates substeps in catalytic swiveling domain mechanism.,Minges A, Hoppner A, Groth G Protein Sci. 2017 May 3. doi: 10.1002/pro.3184. PMID:28470715<ref>PMID:28470715</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5lu4" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Pyruvate, phosphate dikinase]] | ||
| + | [[Category: Groth, G]] | ||
| + | [[Category: Hoeppner, A]] | ||
| + | [[Category: Minges, A]] | ||
| + | [[Category: Conformational transition]] | ||
| + | [[Category: Nucleotide binding]] | ||
| + | [[Category: Phosphotransferase]] | ||
| + | [[Category: Swiveling mechanism]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 13:34, 24 May 2017
C4-type pyruvate phosphate dikinase: conformational intermediate of central domain in the swiveling mechanism
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