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5ohx

From Proteopedia

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Structure of active cystathionine B-synthase from Apis mellifera

Structural highlights

5ohx is a 2 chain structure with sequence from Apis mellifera. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.2Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5ohx"

@@ Line 1: / Line 1: @@
 ==Structure of active cystathionine B-synthase from Apis mellifera==
-<StructureSection load='5ohx' size='340' side='right' caption='[[5ohx]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
+<StructureSection load='5ohx' size='340' side='right'caption='[[5ohx]], [[Resolution|resolution]] 3.20&Aring;' 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>
+<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]] 3.2&#8491;</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='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'>[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>
+== 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;">
 == Publication Abstract from PubMed ==
@@ Line 16: / Line 19: @@
 </div>
 <div class="pdbe-citations 5ohx" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Cystathionine ÃÂ²-synthase 3D structures|Cystathionine ÃÂ²-synthase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Ereno-Orbea, J]]
+[[Category: Apis mellifera]]
-[[Category: Gimenez-Mascarell, P]]
+[[Category: Large Structures]]
-[[Category: Klaudiny, J]]
+[[Category: Ereno-Orbea J]]
-[[Category: Kraus, J P]]
+[[Category: Gimenez-Mascarell P]]
-[[Category: Majtan, J]]
+[[Category: Klaudiny J]]
-[[Category: Majtan, T]]
+[[Category: Kraus JP]]
-[[Category: Martinez-Cruz, L A]]
+[[Category: Majtan J]]
-[[Category: Oyenarte, I]]
+[[Category: Majtan T]]
-[[Category: Adomet]]
+[[Category: Martinez-Cruz LA]]
-[[Category: Cb]]
+[[Category: Oyenarte I]]
-[[Category: H2]]
-[[Category: Homocystinuria]]
-[[Category: Hydrogen sulfide]]
-[[Category: Lyase]]
-[[Category: S-adenosylmethionine]]
-[[Category: Transsulfuration]]

5ohx

From Proteopedia

Current revision

Structure of active cystathionine B-synthase from Apis mellifera

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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