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==Full length structure of cystathionine beta-synthase from Drosophila in complex with serine== | ==Full length structure of cystathionine beta-synthase from Drosophila in complex with serine== | ||
<StructureSection load='3pc4' size='340' side='right' caption='[[3pc4]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='3pc4' size='340' side='right'caption='[[3pc4]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3pc4]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3pc4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PC4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PC4 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=KOU:(E)-N-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYLIDENE)-L-SERINE'>KOU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | </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=KOU:(E)-N-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYLIDENE)-L-SERINE'>KOU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pc2|3pc2]], [[3pc3|3pc3]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3pc2|3pc2]], [[3pc3|3pc3]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CG1753, Dmel_CG1753 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CG1753, Dmel_CG1753 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cystathionine_beta-synthase Cystathionine beta-synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.22 4.2.1.22] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3pc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pc4 OCA], [https://pdbe.org/3pc4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pc4 RCSB], [https://www.ebi.ac.uk/pdbsum/3pc4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pc4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 3pc4" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3pc4" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Cystathionine ò-synthase|Cystathionine ò-synthase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 25: | Line 28: | ||
[[Category: Cystathionine beta-synthase]] | [[Category: Cystathionine beta-synthase]] | ||
[[Category: Drome]] | [[Category: Drome]] | ||
[[Category: Large Structures]] | |||
[[Category: Koutmos, M]] | [[Category: Koutmos, M]] | ||
[[Category: Smith, J L]] | [[Category: Smith, J L]] | ||
Revision as of 11:33, 25 May 2022
Full length structure of cystathionine beta-synthase from Drosophila in complex with serineFull length structure of cystathionine beta-synthase from Drosophila in complex with serine
Structural highlights
Publication 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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