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| | <StructureSection load='5ohx' size='340' side='right'caption='[[5ohx]], [[Resolution|resolution]] 3.20Å' scene=''> | | <StructureSection load='5ohx' size='340' side='right'caption='[[5ohx]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ohx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Apime Apime]. 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> | + | <table><tr><td colspan='2'>[[5ohx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Apis_mellifera Apis mellifera]. 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 [https://proteopedia.org/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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AmCBS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7460 APIME])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ohx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ohx OCA], [https://pdbe.org/5ohx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ohx RCSB], [https://www.ebi.ac.uk/pdbsum/5ohx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ohx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CBS_APIME CBS_APIME] Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L-homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine.<ref>PMID:29275181</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5ohx" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5ohx" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Cystathionine ò-synthase 3D structures|Cystathionine ò-synthase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Apime]] | + | [[Category: Apis mellifera]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ereno-Orbea, J]] | + | [[Category: Ereno-Orbea J]] |
| - | [[Category: Gimenez-Mascarell, P]] | + | [[Category: Gimenez-Mascarell P]] |
| - | [[Category: Klaudiny, J]] | + | [[Category: Klaudiny J]] |
| - | [[Category: Kraus, J P]] | + | [[Category: Kraus JP]] |
| - | [[Category: Majtan, J]] | + | [[Category: Majtan J]] |
| - | [[Category: Majtan, T]] | + | [[Category: Majtan T]] |
| - | [[Category: Martinez-Cruz, L A]] | + | [[Category: Martinez-Cruz LA]] |
| - | [[Category: Oyenarte, I]] | + | [[Category: Oyenarte I]] |
| - | [[Category: Adomet]]
| + | |
| - | [[Category: Cb]]
| + | |
| - | [[Category: H2]]
| + | |
| - | [[Category: Homocystinuria]]
| + | |
| - | [[Category: Hydrogen sulfide]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: S-adenosylmethionine]]
| + | |
| - | [[Category: Transsulfuration]]
| + | |
| Structural highlights
Function
CBS_APIME Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L-homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gimenez-Mascarell P, Majtan T, Oyenarte I, Ereno-Orbea J, Majtan J, Klaudiny J, Kraus JP, Martinez-Cruz LA. Crystal structure of cystathionine beta-synthase from honeybee Apis mellifera. J Struct Biol. 2017 Dec 21. pii: S1047-8477(17)30231-9. doi:, 10.1016/j.jsb.2017.12.008. PMID:29275181 doi:http://dx.doi.org/10.1016/j.jsb.2017.12.008
- ↑ Gimenez-Mascarell P, Majtan T, Oyenarte I, Ereno-Orbea J, Majtan J, Klaudiny J, Kraus JP, Martinez-Cruz LA. Crystal structure of cystathionine beta-synthase from honeybee Apis mellifera. J Struct Biol. 2017 Dec 21. pii: S1047-8477(17)30231-9. doi:, 10.1016/j.jsb.2017.12.008. PMID:29275181 doi:http://dx.doi.org/10.1016/j.jsb.2017.12.008
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