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2f1k

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{{Seed}}
 
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[[Image:2f1k.png|left|200px]]
 
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==Crystal structure of Synechocystis arogenate dehydrogenase==
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The line below this paragraph, containing "STRUCTURE_2f1k", creates the "Structure Box" on the page.
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<StructureSection load='2f1k' size='340' side='right'caption='[[2f1k]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2f1k]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F1K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F1K FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.55&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene>, <scene name='pdbligand=OMT:S-DIOXYMETHIONINE'>OMT</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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{{STRUCTURE_2f1k| PDB=2f1k | SCENE= }}
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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=2f1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f1k OCA], [https://pdbe.org/2f1k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f1k RCSB], [https://www.ebi.ac.uk/pdbsum/2f1k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f1k ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/P73906_SYNY3 P73906_SYNY3]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f1/2f1k_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2f1k ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The extreme diversity in substrate specificity, and in the regulation mechanism of arogenate/prephenate dehydrogenase enzymes in nature, makes a comparative structural study of these enzymes of great interest. We report here on the biochemical and structural characterization of arogenate dehydrogenase from Synechocystis sp. (TyrAsy). This work paves the way for the understanding of the structural determinants leading to diversity in substrate specificity, and of the regulation mechanisms of arogenate/prephenate dehydrogenases. The overall structure of TyrAsy in complex with NADP was refined to 1.6 A. The asymmetric unit contains two TyrAsy homodimers, with each monomer consisting of a nucleotide binding N-terminal domain and a particularly unique alpha-helical C-terminal dimerization domain. The substrate arogenate was modeled into the active site. The model of the ternary complex enzyme-NADP-arogenate nicely reveals at the atomic level the concerted mechanism of the arogenate/prephenate dehydrogenase reaction.
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===Crystal structure of Synechocystis arogenate dehydrogenase===
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Biochemical characterization and crystal structure of Synechocystis arogenate dehydrogenase provide insights into catalytic reaction.,Legrand P, Dumas R, Seux M, Rippert P, Ravelli R, Ferrer JL, Matringe M Structure. 2006 Apr;14(4):767-76. PMID:16615917<ref>PMID:16615917</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_16615917}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2f1k" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16615917 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16615917}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2F1K is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F1K OCA].
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[[Category: Synechocystis sp. PCC 6803]]
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[[Category: Dumas R]]
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==Reference==
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[[Category: Ferrer J-L]]
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<ref group="xtra">PMID:16615917</ref><references group="xtra"/>
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[[Category: Legrand P]]
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[[Category: Arogenate dehydrogenase]]
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[[Category: Matringe M]]
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[[Category: Synechocystis sp.]]
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[[Category: Ravelli R]]
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[[Category: Dumas, R.]]
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[[Category: Rippert P]]
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[[Category: Ferrer, J L.]]
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[[Category: Seux M]]
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[[Category: Legrand, P.]]
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[[Category: Matringe, M.]]
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[[Category: Ravelli, R.]]
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[[Category: Rippert, P.]]
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[[Category: Seux, M.]]
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[[Category: Arogenate/prephenate dehydrogenase]]
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[[Category: Tyrosine synthesis]]
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[[Category: X-ray crystallography structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 04:58:13 2009''
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Current revision

Crystal structure of Synechocystis arogenate dehydrogenase

PDB ID 2f1k

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