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5b3a

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Revision as of 06:37, 31 May 2023

Crystal Structure of O-Phoshoserine Sulfhydrylase from Aeropyrum pernix in Complexed with the alpha-Aminoacrylate Intermediate

Structural highlights

5b3a is a 2 chain structure with sequence from Aeropyrum pernix K1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CYSO_AERPE Cysteine synthase that can also catalyze the synthesis of S-sulfo-L-cysteine from thiosulfate and O(3)-acetyl-L-serine, as well as the sulfhydrylation of L-serine by sulfide.^[1]

Publication Abstract from PubMed

O-Phosphoserine sulfhydrylase (OPSS) synthesizes cysteine from O-phospho-L-serine (OPS) and sulfide. We have determined the three-dimensional structures of OPSS from hyperthermophilic archaeon Aeropyrum pernix K1 (ApOPSS) in complex with aminoacrylate intermediate (AA) formed from pyridoxal 5'-phosphate with OPS or in complex with cysteine and compared them with that of ApOPSS. We found an orientational change of F225 at the active-site entrance and constructed an F225A mutant to examine its activities and AA stability and clarify the role of F225 in ApOPSS. The OPS and O-acetyl-L-serine (OAS) sulfhydrylase activities of the F225A mutant decreased by 4.2- and 15-fold compared to those of the wild-type (wt) ApOPSS, respectively. The ability of OPS and OAS to form AA also decreased by 12- and 27-fold, respectively. AA was less stable in the F225A mutant than in the wt ApOPSS. Simulated docking showed that leaving groups, such as phosphate and acetate, were oriented to the inside of the active site in the F225A mutant, whereas they were oriented to the entrance in the wt ApOPSS. These results suggest that F225 in ApOPSS plays important roles in maintaining the hydrophobic environment of AA from solvent water and in controlling the orientation of leaving groups.

Role of F225 in O-phosphoserine sulfhydrylase from Aeropyrum pernix K1.,Takeda E, Kunimoto K, Kawai Y, Kataoka M, Ishikawa K, Nakamura T Extremophiles. 2016 Jul 5. PMID:27377295^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Mino K, Ishikawa K. Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1. J Bacteriol. 2003 Apr;185(7):2277-84. PMID:12644499
↑ Takeda E, Kunimoto K, Kawai Y, Kataoka M, Ishikawa K, Nakamura T. Role of F225 in O-phosphoserine sulfhydrylase from Aeropyrum pernix K1. Extremophiles. 2016 Jul 5. PMID:27377295 doi:http://dx.doi.org/10.1007/s00792-016-0862-6

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5b3a"

@@ Line 3: / Line 3: @@
 <StructureSection load='5b3a' size='340' side='right'caption='[[5b3a]], [[Resolution|resolution]] 2.14&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5b3a]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aerpe Aerpe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B3A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B3A FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5b3a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeropyrum_pernix_K1 Aeropyrum pernix K1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B3A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B3A FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0JO:2-{[(E)-{3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYLIDENE]AMINO}PROP-2-ENOIC+ACID'>0JO</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0JO:2-{[(E)-{3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYLIDENE]AMINO}PROP-2-ENOIC+ACID'>0JO</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5b36|5b36]]</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=5b3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b3a OCA], [https://pdbe.org/5b3a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b3a RCSB], [https://www.ebi.ac.uk/pdbsum/5b3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b3a ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cysO, APE_1586 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272557 AERPE])</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=5b3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b3a OCA], [http://pdbe.org/5b3a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b3a RCSB], [http://www.ebi.ac.uk/pdbsum/5b3a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b3a ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CYSO_AERPE CYSO_AERPE]] Cysteine synthase that can also catalyze the synthesis of S-sulfo-L-cysteine from thiosulfate and O(3)-acetyl-L-serine, as well as the sulfhydrylation of L-serine by sulfide.<ref>PMID:12644499</ref>
+[https://www.uniprot.org/uniprot/CYSO_AERPE CYSO_AERPE] Cysteine synthase that can also catalyze the synthesis of S-sulfo-L-cysteine from thiosulfate and O(3)-acetyl-L-serine, as well as the sulfhydrylation of L-serine by sulfide.<ref>PMID:12644499</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Aerpe]]
+[[Category: Aeropyrum pernix K1]]
 [[Category: Large Structures]]
-[[Category: Ishikawa, K]]
+[[Category: Ishikawa K]]
-[[Category: Kataoka, M]]
+[[Category: Kataoka M]]
-[[Category: Kawai, Y]]
+[[Category: Kawai Y]]
-[[Category: Nakamura, T]]
+[[Category: Nakamura T]]
-[[Category: Takeda, E]]
+[[Category: Takeda E]]
-[[Category: Cysteine biosynthesis]]
-[[Category: External schiff base of plp with alpha-amino acrylate]]
-[[Category: Intermediate]]
-[[Category: Sulfhydrylase]]
-[[Category: Transferase]]

5b3a

From Proteopedia

Revision as of 06:37, 31 May 2023

Crystal Structure of O-Phoshoserine Sulfhydrylase from Aeropyrum pernix in Complexed with the alpha-Aminoacrylate Intermediate

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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