5ohx: Difference between revisions
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==Structure of active cystathionine B-synthase from Apis mellifera== | |||
<StructureSection load='5ohx' size='340' side='right' caption='[[5ohx]], [[Resolution|resolution]] 3.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ohx]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OHX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OHX FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><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></td></tr> | |||
<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=5ohx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ohx OCA], [http://pdbe.org/5ohx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ohx RCSB], [http://www.ebi.ac.uk/pdbsum/5ohx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ohx ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cystathionine beta-synthase (CBS), the key enzyme in the transsulfuration pathway, links methionine metabolism to the biosynthesis of cellular redox controlling molecules. CBS catalyzes the pyridoxal-5'-phosphate-dependent condensation of serine and homocysteine to form cystathionine, which is subsequently converted into cysteine. Besides maintaining cellular sulfur amino acid homeostasis, CBS also catalyzes multiple hydrogen sulfide-generating reactions using cysteine and homocysteine as substrates. In mammals, CBS is activated by S-adenosylmethionine (AdoMet), where it can adopt two different conformations (basal and activated), but exists as a unique highly active species in fruit fly Drosophila melanogaster. Here we present the crystal structure of CBS from honeybey Apis mellifera, which shows a constitutively active dimeric species and let explain why the enzyme is not allosterically regulated by AdoMet. In addition, comparison of available CBS structures unveils a substrate-induced closure of the catalytic cavity, which in humans is affected by the AdoMet-dependent regulation and likely impaired by the homocystinuria causing mutation T191M. | |||
Crystal structure of cystathionine beta-synthase from honeybee Apis mellifera.,Gimenez-Mascarell P, Majtan T, Oyenarte I, Ereno-Orbea J, Majtan J, Klaudiny J, Kraus JP, Martinez-Cruz LA J Struct Biol. 2017 Dec 21. pii: S1047-8477(17)30231-9. doi:, 10.1016/j.jsb.2017.12.008. PMID:29275181<ref>PMID:29275181</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5ohx" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ereno-Orbea, J]] | |||
[[Category: Gimenez-Mascarell, P]] | [[Category: Gimenez-Mascarell, P]] | ||
[[Category: Klaudiny, J]] | [[Category: Klaudiny, J]] | ||
[[Category: Kraus, J | [[Category: Kraus, J P]] | ||
[[Category: Majtan, J]] | |||
[[Category: Majtan, T]] | [[Category: Majtan, T]] | ||
[[Category: Martinez-Cruz, L | [[Category: Martinez-Cruz, L A]] | ||
[[Category: Oyenarte, I]] | [[Category: Oyenarte, I]] | ||
[[Category: Adomet]] | |||
[[Category: Cb]] | |||
[[Category: H2]] | |||
[[Category: Homocystinuria]] | |||
[[Category: Hydrogen sulfide]] | |||
[[Category: Lyase]] | |||
[[Category: S-adenosylmethionine]] | |||
[[Category: Transsulfuration]] | |||
