9khn

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'''Unreleased structure'''
 
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The entry 9khn is ON HOLD
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==Crystal structure of human cystathionine gamma-lyase in complex with L-aminoethoxyvinylglycine==
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<StructureSection load='9khn' size='340' side='right'caption='[[9khn]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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Authors: Kukimoto-Niino, M., Shirouzu, M.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9khn]] 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=9KHN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9KHN FirstGlance]. <br>
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Description: Crystal structure of human cystathionine gamma-lyase in complex with L-aminoethoxyvinylglycine
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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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[[Category: Unreleased Structures]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PPG:(2E,3E)-4-(2-AMINOETHOXY)-2-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)IMINO]BUT-3-ENOIC+ACID'>PPG</scene></td></tr>
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[[Category: Kukimoto-Niino, M]]
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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=9khn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9khn OCA], [https://pdbe.org/9khn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9khn RCSB], [https://www.ebi.ac.uk/pdbsum/9khn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9khn ProSAT]</span></td></tr>
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[[Category: Shirouzu, M]]
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/CGL_HUMAN CGL_HUMAN] Defects in CTH are the cause of cystathioninuria (CSTNU) [MIM:[https://omim.org/entry/219500 219500]. It is an autosomal recessive phenotype characterized by abnormal accumulation of plasma cystathionine, leading to increased urinary excretion.<ref>PMID:18476726</ref> <ref>PMID:12574942</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/CGL_HUMAN CGL_HUMAN] Catalyzes the last step in the trans-sulfuration pathway from methionine to cysteine. Has broad substrate specificity. Converts cystathionine to cysteine, ammonia and 2-oxobutanoate. Converts two cysteine molecules to lanthionine and hydrogen sulfide. Can also accept homocysteine as substrate. Specificity depends on the levels of the endogenous substrates. Generates the endogenous signaling molecule hydrogen sulfide (H2S), and so contributes to the regulation of blood pressure. Acts as a cysteine-protein sulfhydrase by mediating sulfhydration of target proteins: sulfhydration consists of converting -SH groups into -SSH on specific cysteine residues of target proteins such as GAPDH, PTPN1 and NF-kappa-B subunit RELA, thereby regulating their function.<ref>PMID:19261609</ref> <ref>PMID:22169477</ref> <ref>PMID:19019829</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Kukimoto-Niino M]]
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[[Category: Shirouzu M]]

Current revision

Crystal structure of human cystathionine gamma-lyase in complex with L-aminoethoxyvinylglycine

PDB ID 9khn

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