3ezw

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{{Seed}}
 
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[[Image:3ezw.jpg|left|200px]]
 
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==Crystal Structure of a Hyperactive Escherichia coli Glycerol Kinase Mutant Gly230 --> Asp Obtained Using Microfluidic Crystallization Devices==
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The line below this paragraph, containing "STRUCTURE_3ezw", creates the "Structure Box" on the page.
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<StructureSection load='3ezw' size='340' side='right'caption='[[3ezw]], [[Resolution|resolution]] 2.00&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'>[[3ezw]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2p3r 2p3r]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EZW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EZW 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]] 2&#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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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{{STRUCTURE_3ezw| PDB=3ezw | 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=3ezw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ezw OCA], [https://pdbe.org/3ezw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ezw RCSB], [https://www.ebi.ac.uk/pdbsum/3ezw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ezw ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GLPK_ECOLI GLPK_ECOLI] Key enzyme in the regulation of glycerol uptake and metabolism.[HAMAP-Rule:MF_00186]
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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/ez/3ezw_consurf.spt"</scriptWhenChecked>
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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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</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=3ezw 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 crystal structure of an Escherichia coli glycerol kinase mutant Gly230 --&gt; Asp (GKG230D) was determined to 2.0 A resolution using a microfluidics based crystallization platform. The crystallization strategy involved a suite of microfluidic devices that characterized the solubility trends of GKG230D, performed nanoliter volume free interface diffusion crystallization experiments, and produced diffraction-quality crystals for in situ data collection. GKG230D displays increased enzymatic activity and decreased allosteric regulation by the glycolytic pathway intermediate fructose 1,6-bisphosphate (FBP) compared to wild-type GK (GKWT). Structural analysis revealed that the decreased allosteric regulation is a result of the altered FBP binding loop conformations in GKG230D that interfere with the wild-type FBP binding site. The altered FBP binding loop conformations in GKG230D are supported through a series of intramolecular loop interactions. The appearance of Asp230 in the FBP binding loops also repositions the wild-type FBP binding residues away from the FBP binding site. Light scattering analysis confirmed GKG230D is a dimer and is resistant to tetramer formation in the presence of FBP, whereas GKWT dimers are converted into putatively inactive tetramers in the presence of FBP. GKG230D also provides the first structural evidence for multiple GK monomer conformations in the presence of glycerol and in the absence of a nucleotide substrate and verifies that glycerol binding is not responsible for locking GK into the closed conformation necessary for GK activity.
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===Crystal Structure of a Hyperactive Escherichia coli Glycerol Kinase Mutant Gly230 --> Asp Obtained Using Microfluidic Crystallization Devices===
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Crystal structure of a hyperactive Escherichia coli glycerol kinase mutant Gly230 --&gt; Asp obtained using microfluidic crystallization devices.,Anderson MJ, DeLabarre B, Raghunathan A, Palsson BO, Brunger AT, Quake SR Biochemistry. 2007 May 15;46(19):5722-31. Epub 2007 Apr 19. PMID:17441732<ref>PMID:17441732</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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<div class="pdbe-citations 3ezw" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_17441732}}, adds the Publication Abstract to the page
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*[[Glycerol kinase|Glycerol kinase]]
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(as it appears on PubMed at http://www.pubmed.gov), where 17441732 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17441732}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Escherichia coli K-12]]
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3EZW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2p3r 2p3r]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EZW OCA].
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[[Category: Large Structures]]
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[[Category: Anderson MJ]]
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==Reference==
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[[Category: Brunger AT]]
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Crystal structure of a hyperactive Escherichia coli glycerol kinase mutant Gly230 --&gt; Asp obtained using microfluidic crystallization devices., Anderson MJ, DeLabarre B, Raghunathan A, Palsson BO, Brunger AT, Quake SR, Biochemistry. 2007 May 15;46(19):5722-31. Epub 2007 Apr 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17441732 17441732]
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[[Category: DeLaBarre B]]
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[[Category: Escherichia coli]]
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[[Category: Dunten P]]
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[[Category: Glycerol kinase]]
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[[Category: Quake SR]]
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[[Category: Single protein]]
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[[Category: Anderson, M J.]]
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[[Category: Brunger, A T.]]
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[[Category: DeLaBarre, B.]]
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[[Category: Dunten, P.]]
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[[Category: Quake, S R.]]
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[[Category: Allosteric regulation]]
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[[Category: Atp-binding]]
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[[Category: Crystal structure]]
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[[Category: Glycerol kinase]]
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[[Category: Glycerol metabolism]]
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[[Category: In situ data collection]]
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[[Category: Kinase]]
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[[Category: Metal-binding]]
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[[Category: Microfluidic]]
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[[Category: Nucleotide-binding]]
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[[Category: Transferase]]
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[[Category: Zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 5 11:55:57 2008''
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Current revision

Crystal Structure of a Hyperactive Escherichia coli Glycerol Kinase Mutant Gly230 --> Asp Obtained Using Microfluidic Crystallization Devices

PDB ID 3ezw

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