1jbq
From Proteopedia
(Difference between revisions)
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| - | + | ==STRUCTURE OF HUMAN CYSTATHIONINE BETA-SYNTHASE: A UNIQUE PYRIDOXAL 5'-PHOSPHATE DEPENDENT HEMEPROTEIN== | |
| - | + | <StructureSection load='1jbq' size='340' side='right' caption='[[1jbq]], [[Resolution|resolution]] 2.60Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1jbq]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JBQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JBQ FirstGlance]. <br> | |
| - | ==Disease== | + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene><br> |
| - | [[http://www.uniprot.org/uniprot/CBS_HUMAN CBS_HUMAN]] Defects in CBS are the cause of cystathionine beta-synthase deficiency (CBSD) [MIM:[http://omim.org/entry/236200 236200]]. CBSD is an enzymatic deficiency resulting in altered sulfur metabolism and homocystinuria. The clinical features of untreated homocystinuria due to CBS deficiency include myopia, ectopia lentis, mental retardation, skeletal anomalies resembling Marfan syndrome, and thromboembolic events. Light skin and hair can also be present. Biochemical features include increased urinary homocystine and methionine.<ref>PMID:1301198</ref><ref>PMID:8353501</ref><ref>PMID:7506602</ref><ref>PMID:7981678</ref><ref>PMID:7849717</ref><ref>PMID:7967489</ref><ref>PMID:7611293</ref><ref>PMID:7762555</ref><ref>PMID:7635485</ref><ref>PMID:8528202</ref><ref>PMID:7564249</ref><ref>PMID:8755636</ref><ref>PMID:8803779</ref><ref>PMID:9156316</ref><ref>PMID:9361025</ref><ref>PMID:8990018</ref><ref>PMID:9266356</ref><ref>PMID:10462600</ref><ref>PMID:10215408</ref><ref>PMID:9889017</ref><ref>PMID:10408774</ref><ref>PMID:11013450</ref><ref>PMID:11359213</ref><ref>PMID:11553052</ref><ref>PMID:12007221</ref><ref>PMID:12124992</ref><ref>PMID:12815602</ref><ref>PMID:14635102</ref><ref>PMID:15146473</ref><ref>PMID:15365998</ref><ref>PMID:15993874</ref><ref>PMID:16205833</ref><ref>PMID:16429402</ref><ref>PMID:21520339</ref><ref>PMID:21240075</ref> | + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1d6s|1d6s]]</td></tr> |
| - | + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cystathionine_beta-synthase Cystathionine beta-synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.22 4.2.1.22] </span></td></tr> | |
| - | ==Function== | + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jbq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jbq RCSB], [http://www.ebi.ac.uk/pdbsum/1jbq PDBsum]</span></td></tr> |
| + | <table> | ||
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/CBS_HUMAN CBS_HUMAN]] Defects in CBS are the cause of cystathionine beta-synthase deficiency (CBSD) [MIM:[http://omim.org/entry/236200 236200]]. CBSD is an enzymatic deficiency resulting in altered sulfur metabolism and homocystinuria. The clinical features of untreated homocystinuria due to CBS deficiency include myopia, ectopia lentis, mental retardation, skeletal anomalies resembling Marfan syndrome, and thromboembolic events. Light skin and hair can also be present. Biochemical features include increased urinary homocystine and methionine.<ref>PMID:1301198</ref> <ref>PMID:8353501</ref> <ref>PMID:7506602</ref> <ref>PMID:7981678</ref> <ref>PMID:7849717</ref> <ref>PMID:7967489</ref> <ref>PMID:7611293</ref> <ref>PMID:7762555</ref> <ref>PMID:7635485</ref> <ref>PMID:8528202</ref> <ref>PMID:7564249</ref> <ref>PMID:8755636</ref> <ref>PMID:8803779</ref> <ref>PMID:9156316</ref> <ref>PMID:9361025</ref> <ref>PMID:8990018</ref> <ref>PMID:9266356</ref> <ref>PMID:10462600</ref> <ref>PMID:10215408</ref> <ref>PMID:9889017</ref> <ref>PMID:10408774</ref> <ref>PMID:11013450</ref> <ref>PMID:11359213</ref> <ref>PMID:11553052</ref> <ref>PMID:12007221</ref> <ref>PMID:12124992</ref> <ref>PMID:12815602</ref> <ref>PMID:14635102</ref> <ref>PMID:15146473</ref> <ref>PMID:15365998</ref> <ref>PMID:15993874</ref> <ref>PMID:16205833</ref> <ref>PMID:16429402</ref> <ref>PMID:21520339</ref> <ref>PMID:21240075</ref> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/CBS_HUMAN CBS_HUMAN]] Only known pyridoxal phosphate-dependent enzyme that contains heme. Important regulator of hydrogen sulfide, especially in the brain, utilizing cysteine instead of serine to catalyze the formation of hydrogen sulfide. Hydrogen sulfide is a gastratransmitter with signaling and cytoprotective effects such as acting as a neuromodulator in the brain to protect neurons against hypoxic injury (By similarity). | [[http://www.uniprot.org/uniprot/CBS_HUMAN CBS_HUMAN]] Only known pyridoxal phosphate-dependent enzyme that contains heme. Important regulator of hydrogen sulfide, especially in the brain, utilizing cysteine instead of serine to catalyze the formation of hydrogen sulfide. Hydrogen sulfide is a gastratransmitter with signaling and cytoprotective effects such as acting as a neuromodulator in the brain to protect neurons against hypoxic injury (By similarity). | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jb/1jbq_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cystathionine beta-synthase (CBS) is a unique heme- containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Here we present the X-ray crystal structure of a truncated form of the enzyme. CBS shares the same fold with O-acetylserine sulfhydrylase but it contains an additional N-terminal heme binding site. This heme binding motif together with a spatially adjacent oxidoreductase active site motif could explain the regulation of its enzyme activity by redox changes. | ||
| - | + | Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein.,Meier M, Janosik M, Kery V, Kraus JP, Burkhard P EMBO J. 2001 Aug 1;20(15):3910-6. PMID:11483494<ref>PMID:11483494</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Cystathionine beta-synthase]] | [[Category: Cystathionine beta-synthase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
Revision as of 16:13, 29 September 2014
STRUCTURE OF HUMAN CYSTATHIONINE BETA-SYNTHASE: A UNIQUE PYRIDOXAL 5'-PHOSPHATE DEPENDENT HEMEPROTEIN
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