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2d33

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[[Image:2d33.gif|left|200px]]
 
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{{Structure
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==Crystal Structure of gamma-Glutamylcysteine Synthetase Complexed with Aluminum Fluoride==
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|PDB= 2d33 |SIZE=350|CAPTION= <scene name='initialview01'>2d33</scene>, resolution 2.60&Aring;
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<StructureSection load='2d33' size='340' side='right'caption='[[2d33]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> and <scene name='pdbligand=AF3:ALUMINUM FLUORIDE'>AF3</scene>
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<table><tr><td colspan='2'>[[2d33]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D33 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D33 FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Glutamate--cysteine_ligase Glutamate--cysteine ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.2 6.3.2.2]
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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]] 2.6&#8491;</td></tr>
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|GENE= gshI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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<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=AF3:ALUMINUM+FLUORIDE'>AF3</scene>, <scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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}}
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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=2d33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d33 OCA], [https://pdbe.org/2d33 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d33 RCSB], [https://www.ebi.ac.uk/pdbsum/2d33 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d33 ProSAT]</span></td></tr>
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</table>
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'''Crystal Structure of gamma-Glutamylcysteine Synthetase Complexed with Aluminum Fluoride'''
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== Function ==
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[https://www.uniprot.org/uniprot/GSH1_ECOLI GSH1_ECOLI]
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Gamma-glutamylcysteine synthetase (gammaGCS), a rate-limiting enzyme in glutathione biosynthesis, plays a central role in glutathione homeostasis and is a target for development of potential therapeutic agents against parasites and cancer. We have determined the crystal structures of Escherichia coli gammaGCS unliganded and complexed with a sulfoximine-based transition-state analog inhibitor at resolutions of 2.5 and 2.1 A, respectively. In the crystal structure of the complex, the bound inhibitor is phosphorylated at the sulfoximido nitrogen and is coordinated to three Mg2+ ions. The cysteine-binding site was identified; it is formed inductively at the transition state. In the unliganded structure, an open space exists around the representative cysteine-binding site and is probably responsible for the competitive binding of glutathione. Upon inhibitor binding, the side chains of Tyr-241 and Tyr-300 turn, forming a hydrogen-bonding triad with the carboxyl group of the inhibitor's cysteine moiety, allowing this moiety to fit tightly into the cysteine-binding site with concomitant accommodation of its side chain into a shallow pocket. This movement is caused by a conformational change of a switch loop (residues 240-249). Based on this crystal structure, the cysteine-binding sites of mammalian and parasitic gammaGCSs were predicted by multiple sequence alignment, although no significant sequence identity exists between the E. coli gammaGCS and its eukaryotic homologues. The identification of this cysteine-binding site provides important information for the rational design of novel gammaGCS inhibitors.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d3/2d33_consurf.spt"</scriptWhenChecked>
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2D33 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D33 OCA].
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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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==Reference==
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</jmolCheckbox>
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Crystal structure of gamma-glutamylcysteine synthetase: insights into the mechanism of catalysis by a key enzyme for glutathione homeostasis., Hibi T, Nii H, Nakatsu T, Kimura A, Kato H, Hiratake J, Oda J, Proc Natl Acad Sci U S A. 2004 Oct 19;101(42):15052-7. Epub 2004 Oct 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15477603 15477603]
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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=2d33 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Glutamate--cysteine ligase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Hibi T]]
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[[Category: Hibi, T.]]
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[[Category: Katano H]]
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[[Category: Katano, H.]]
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[[Category: Kurokawa Y]]
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[[Category: Kurokawa, Y.]]
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[[Category: Nakayama M]]
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[[Category: Nakayama, M.]]
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[[Category: Nii H]]
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[[Category: Nii, H.]]
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[[Category: Oda J]]
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[[Category: Oda, J.]]
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[[Category: ADP]]
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[[Category: AF3]]
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[[Category: CYS]]
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[[Category: GLU]]
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[[Category: MG]]
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[[Category: glutathione homeostasis]]
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[[Category: peptide synthesis]]
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[[Category: phosphoryl transfer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:22:43 2008''
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Current revision

Crystal Structure of gamma-Glutamylcysteine Synthetase Complexed with Aluminum Fluoride

PDB ID 2d33

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