3pc3: Difference between revisions
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< | ==Full length structure of cystathionine beta-synthase from Drosophila in complex with aminoacrylate== | ||
<StructureSection load='3pc3' size='340' side='right'caption='[[3pc3]], [[Resolution|resolution]] 1.55Å' scene=''> | |||
== Structural highlights == | |||
or the | <table><tr><td colspan='2'>[[3pc3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PC3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PC3 FirstGlance]. <br> | ||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55Å</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=P1T:2-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)AMINO]ACRYLIC+ACID'>P1T</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=3pc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pc3 OCA], [https://pdbe.org/3pc3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pc3 RCSB], [https://www.ebi.ac.uk/pdbsum/3pc3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pc3 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9VRD9_DROME Q9VRD9_DROME] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The catalytic potential for H(2)S biogenesis and homocysteine clearance converge at the active site of cystathionine beta-synthase (CBS), a pyridoxal phosphate-dependent enzyme. CBS catalyzes beta-replacement reactions of either serine or cysteine by homocysteine to give cystathionine and water or H(2)S, respectively. In this study, high-resolution structures of the full-length enzyme from Drosophila in which a carbanion (1.70 A) and an aminoacrylate intermediate (1.55 A) have been captured are reported. Electrostatic stabilization of the zwitterionic carbanion intermediate is afforded by the close positioning of an active site lysine residue that is initially used for Schiff base formation in the internal aldimine and later as a general base. Additional stabilizing interactions between active site residues and the catalytic intermediates are observed. Furthermore, the structure of the regulatory "energy-sensing" CBS domains, named after this protein, suggests a mechanism for allosteric activation by S-adenosylmethionine. | |||
Structural basis for substrate activation and regulation by cystathionine beta-synthase (CBS) domains in cystathionine {beta}-synthase.,Koutmos M, Kabil O, Smith JL, Banerjee R Proc Natl Acad Sci U S A. 2010 Nov 16. PMID:21081698<ref>PMID:21081698</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3pc3" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cystathionine ò-synthase 3D structures|Cystathionine ò-synthase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
[[ | |||
== | |||
< | |||
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Koutmos | [[Category: Large Structures]] | ||
[[Category: Smith | [[Category: Koutmos M]] | ||
[[Category: Smith JL]] | |||
Latest revision as of 12:51, 6 September 2023
Full length structure of cystathionine beta-synthase from Drosophila in complex with aminoacrylateFull length structure of cystathionine beta-synthase from Drosophila in complex with aminoacrylate
Structural highlights
FunctionPublication Abstract from PubMedThe catalytic potential for H(2)S biogenesis and homocysteine clearance converge at the active site of cystathionine beta-synthase (CBS), a pyridoxal phosphate-dependent enzyme. CBS catalyzes beta-replacement reactions of either serine or cysteine by homocysteine to give cystathionine and water or H(2)S, respectively. In this study, high-resolution structures of the full-length enzyme from Drosophila in which a carbanion (1.70 A) and an aminoacrylate intermediate (1.55 A) have been captured are reported. Electrostatic stabilization of the zwitterionic carbanion intermediate is afforded by the close positioning of an active site lysine residue that is initially used for Schiff base formation in the internal aldimine and later as a general base. Additional stabilizing interactions between active site residues and the catalytic intermediates are observed. Furthermore, the structure of the regulatory "energy-sensing" CBS domains, named after this protein, suggests a mechanism for allosteric activation by S-adenosylmethionine. Structural basis for substrate activation and regulation by cystathionine beta-synthase (CBS) domains in cystathionine {beta}-synthase.,Koutmos M, Kabil O, Smith JL, Banerjee R Proc Natl Acad Sci U S A. 2010 Nov 16. PMID:21081698[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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