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1l9x

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(New page: 200px<br /> <applet load="1l9x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l9x, resolution 1.6&Aring;" /> '''Structure of gamma-G...)
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[[Image:1l9x.gif|left|200px]]<br />
 
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<applet load="1l9x" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1l9x, resolution 1.6&Aring;" />
 
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'''Structure of gamma-Glutamyl Hydrolase'''<br />
 
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==Overview==
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==Structure of gamma-Glutamyl Hydrolase==
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gamma-Glutamyl hydrolase catalyzes the cleavage of the gamma-glutamyl, chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in, folyl and antifolyl poly-gamma-glutamate metabolism. The crystal structure, of human gamma-glutamyl hydrolase, determined at 1.6-A resolution, reveals, that the protein is a homodimer. The overall structure of human, gamma-glutamyl hydrolase contains 11 alpha-helices and 14 beta-strands, with a fold in which a central eight-stranded beta-sheet is sandwiched by, three and five alpha-helices on each side. The topology is very similar to, that of the class I glutamine amidotransferase domains, with the only, major differences consisting of extensions in four loops and at the C, terminus. These insertions are important for defining the substrate, binding cleft and/or the dimer interface. Two sequence motifs are found in, common between human gamma-glutamyl hydrolase and the class I glutamine, amidotransferase family and include the catalytically essential residues, Cys-110 and His-220. These residues are located in the center of a large, l-shaped cleft that is closed at one end and open at the other. Several, conserved residues, including Glu-114, His-171, Gln-218, and Lys-223, may, be important for substrate binding. Modeling of a methotrexate thioester, intermediate, based on the corresponding complex of the glutamate, thioester intermediate of Escherichia coli carbamoyl-phosphate synthetase, indicates that the substrate binds in an orientation with the pteroyl, group toward the open end of the cleft.
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<StructureSection load='1l9x' size='340' side='right'caption='[[1l9x]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1l9x]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L9X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L9X FirstGlance]. <br>
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1L9X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with BME as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Gamma-glutamyl_hydrolase Gamma-glutamyl hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.9 3.4.19.9] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L9X OCA].
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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]] 1.6&#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=BME:BETA-MERCAPTOETHANOL'>BME</scene></td></tr>
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==Reference==
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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=1l9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l9x OCA], [https://pdbe.org/1l9x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l9x RCSB], [https://www.ebi.ac.uk/pdbsum/1l9x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l9x ProSAT]</span></td></tr>
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Three-dimensional structure of human gamma -glutamyl hydrolase. A class I glatamine amidotransferase adapted for a complex substate., Li H, Ryan TJ, Chave KJ, Van Roey P, J Biol Chem. 2002 Jul 5;277(27):24522-9. Epub 2002 Apr 12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11953431 11953431]
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</table>
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[[Category: Gamma-glutamyl hydrolase]]
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== Function ==
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[https://www.uniprot.org/uniprot/GGH_HUMAN GGH_HUMAN] Hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates. Progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha-glutamate (folic acid) and free glutamate. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates.
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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/l9/1l9x_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=1l9x ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Chave, K.J.]]
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[[Category: Chave KJ]]
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[[Category: Li, H.]]
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[[Category: Li H]]
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[[Category: Roey, P.Van.]]
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[[Category: Ryan TJ]]
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[[Category: Ryan, T.J.]]
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[[Category: Van Roey P]]
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[[Category: BME]]
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[[Category: gamma-glutamyl hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:58:09 2007''
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Current revision

Structure of gamma-Glutamyl Hydrolase

PDB ID 1l9x

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