6nba

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'''Unreleased structure'''
 
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The entry 6nba is ON HOLD until Paper Publication
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==Crystal structure of Human Cystathionine gamma lyase with S-3-Carboxpropyl-L-Cysteine==
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<StructureSection load='6nba' size='340' side='right'caption='[[6nba]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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Authors: Kim, H., Yadav, P.K., Banerjee, R., Cho, U.-S.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6nba]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NBA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NBA FirstGlance]. <br>
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Description: Crystal structure of Human Cystathionine gamma lyase with S-3-Carboxpropyl-L-Cysteine
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=P1T:2-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)AMINO]ACRYLIC+ACID'>P1T</scene></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cystathionine_gamma-lyase Cystathionine gamma-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.1 4.4.1.1] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6nba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nba OCA], [http://pdbe.org/6nba PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nba RCSB], [http://www.ebi.ac.uk/pdbsum/6nba PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nba ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[[http://www.uniprot.org/uniprot/CGL_HUMAN CGL_HUMAN]] Defects in CTH are the cause of cystathioninuria (CSTNU) [MIM:[http://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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[[http://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: Cystathionine gamma-lyase]]
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[[Category: Large Structures]]
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[[Category: Banerjee, R]]
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[[Category: Cho, U S]]
[[Category: Kim, H]]
[[Category: Kim, H]]
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[[Category: Banerjee, R]]
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[[Category: Yadav, P K]]
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[[Category: Cho, U.-S]]
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[[Category: Complex]]
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[[Category: Yadav, P.K]]
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[[Category: Lyase]]

Revision as of 05:40, 12 June 2019

Crystal structure of Human Cystathionine gamma lyase with S-3-Carboxpropyl-L-Cysteine

PDB ID 6nba

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