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6l0q

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Crystal Structure of the O-Phosphoserine Sulfhydrylase from Aeropyrum pernix Complexed with O-Phosphoserine

Structural highlights

6l0q is a 4 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.
Method:	X-ray diffraction, Resolution 1.58Å
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

Pyridoxal-5'-phosphate-dependent cysteine synthases synthesize l-cysteine from their primary substrates, O-acetyl-l-serine (OAS) and O-phospho-l-serine (OPS), and their secondary substrate, sulfide. The mechanism by which cysteine synthases recognize OPS remains unclear; hence, we investigated the OPS recognition mechanism of the OPS sulfhydrylase obtained from Aeropyrum pernix K1 (ApOPSS) and the OAS sulfhydrylase-B obtained from Escherichia coli (EcOASS-B), using protein engineering methods. From the amino acid sequence alignment data, we found that some OPS sulfhydrylases (OPSSs) had a Tyr corresponding to the Phe225 and Phe141 residues in ApOPSS and EcOASS-B, respectively, and that the Tyr residue could facilitate OPS recognition. The enzymatic activity of the ApOPSS F225Y mutant toward OPS decreased compared with that of the wild-type; the kcat value decreased 2.3-fold during cysteine synthesis. X-ray crystallography results of the complex of ApOPSS F225Y and F225Y/R297A mutants bound to OPS and l-cysteine showed that kcat might have decreased because of the stronger interactions of the reaction product phosphate with Tyr225, Thr203, and Arg297, and that of the l-cysteine with Tyr225. The specific activity of the EcOASS-B F141Y mutant toward OPS increased by 50-fold compared with that of the wild-type. Thus, a Tyr within a cysteine synthase corresponding to the Phe225 in ApOPSS and Phe141 in EcOASS-B could act as a key residue for classifying an unknown cysteine synthase as an OPSS. The elucidation of the substrate recognition system of cysteine synthases would enable us to effectively classify cysteine synthases and develop pathogen-specific drug targets, as OPSS is absent in mammalian hosts.

Identification of amino acid residues important for recognition of O-phospho-l-serine substrates by cysteine synthase.,Takeda E, Matsui E, Kiryu T, Nakagawa T, Nakabayashi M, Ishikawa K, Nakamura T J Biosci Bioeng. 2021 Feb 6. pii: S1389-1723(21)00003-7. doi:, 10.1016/j.jbiosc.2021.01.003. PMID:33563496^[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, Matsui E, Kiryu T, Nakagawa T, Nakabayashi M, Ishikawa K, Nakamura T. Identification of amino acid residues important for recognition of O-phospho-l-serine substrates by cysteine synthase. J Biosci Bioeng. 2021 Feb 6. pii: S1389-1723(21)00003-7. doi:, 10.1016/j.jbiosc.2021.01.003. PMID:33563496 doi:http://dx.doi.org/10.1016/j.jbiosc.2021.01.003

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/6l0q"

@@ Line 3: / Line 3: @@
 <StructureSection load='6l0q' size='340' side='right'caption='[[6l0q]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6l0q]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aerpe Aerpe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L0Q FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6l0q]] is a 4 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=6L0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L0Q FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=E1U:(2S)-2-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]-3-phosphonooxy-propanoic+acid'>E1U</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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]] 1.58&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cysO, APE_1586 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272557 AERPE])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=E1U:(2S)-2-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]-3-phosphonooxy-propanoic+acid'>E1U</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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=6l0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l0q OCA], [https://pdbe.org/6l0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l0q RCSB], [https://www.ebi.ac.uk/pdbsum/6l0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l0q ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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>
+[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 23: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Aerpe]]
+[[Category: Aeropyrum pernix K1]]
 [[Category: Large Structures]]
-[[Category: Ishikawa, K]]
+[[Category: Ishikawa K]]
-[[Category: Nakabayashi, M]]
+[[Category: Nakabayashi M]]
-[[Category: Nakamura, T]]
+[[Category: Nakamura T]]
-[[Category: Takeda, E]]
+[[Category: Takeda E]]
-[[Category: Cysteine biosynthesis]]
-[[Category: Sulfhydrylase]]
-[[Category: Transferase]]

6l0q

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Current revision

Crystal Structure of the O-Phosphoserine Sulfhydrylase from Aeropyrum pernix Complexed with O-Phosphoserine

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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