2p3r
From Proteopedia
(New page: 200px<br /><applet load="2p3r" size="450" color="white" frame="true" align="right" spinBox="true" caption="2p3r, resolution 2.00Å" /> '''Crystal structure of...) |
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| - | [[Image:2p3r.gif|left|200px]]<br /><applet load="2p3r" size=" | + | [[Image:2p3r.gif|left|200px]]<br /><applet load="2p3r" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2p3r, resolution 2.00Å" /> | caption="2p3r, resolution 2.00Å" /> | ||
'''Crystal structure of a hyperactive Escherichia coli glycerol kinase mutant Gly230->Asp obtained using microfluidic crystallization devices'''<br /> | '''Crystal structure of a hyperactive Escherichia coli glycerol kinase mutant Gly230->Asp obtained using microfluidic crystallization devices'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2P3R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glycerol_kinase Glycerol kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.30 2.7.1.30] Full crystallographic information is available from [http:// | + | 2P3R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glycerol_kinase Glycerol kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.30 2.7.1.30] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P3R OCA]. |
==Reference== | ==Reference== | ||
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[[Category: microfluidics]] | [[Category: microfluidics]] | ||
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Revision as of 13:17, 23 January 2008
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Crystal structure of a hyperactive Escherichia coli glycerol kinase mutant Gly230->Asp obtained using microfluidic crystallization devices
Overview
The crystal structure of an Escherichia coli glycerol kinase mutant Gly230, --> 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.
About this Structure
2P3R is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Glycerol kinase, with EC number 2.7.1.30 Full crystallographic information is available from OCA.
Reference
Crystal Structure of a Hyperactive Escherichia coli Glycerol Kinase Mutant Gly230 --> Asp Obtained Using Microfluidic Crystallization Devices(,)., Anderson MJ, Delabarre B, Raghunathan A, Palsson BO, Brunger AT, Quake SR, Biochemistry. 2007 May 15;46(19):5722-5731. Epub 2007 Apr 19. PMID:17441732
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