5b36 - Revision history

OCA at 15:58, 8 November 2023

OCA — Wed, 08 Nov 2023 15:58:41 GMT

←Older revision		Revision as of 15:58, 8 November 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5b36]] 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=5B36 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B36 FirstGlance]. <br>		<table><tr><td colspan='2'>[[5b36]] 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=5B36 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B36 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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]] 2.15Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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=5b36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b36 OCA], [https://pdbe.org/5b36 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b36 RCSB], [https://www.ebi.ac.uk/pdbsum/5b36 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b36 ProSAT]</span></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=5b36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b36 OCA], [https://pdbe.org/5b36 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b36 RCSB], [https://www.ebi.ac.uk/pdbsum/5b36 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b36 ProSAT]</span></td></tr>
	</table>		</table>

OCA at 06:37, 31 May 2023

OCA — Wed, 31 May 2023 06:37:20 GMT

←Older revision		Revision as of 06:37, 31 May 2023
Line 3:		Line 3:
	<StructureSection load='5b36' size='340' side='right'caption='[[5b36]], [[Resolution\|resolution]] 2.15Å' scene=''>		<StructureSection load='5b36' size='340' side='right'caption='[[5b36]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5b36]] 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=5B36 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5B36 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5b36]] 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=5B36 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B36 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5b3a\|5b3a]]</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=5b36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b36 OCA], [https://pdbe.org/5b36 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b36 RCSB], [https://www.ebi.ac.uk/pdbsum/5b36 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b36 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=5b36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b36 OCA], [~~http~~://pdbe.org/5b36 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5b36 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5b36 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5b36 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== 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;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Aerpe~~]]	+	[[Category: Aeropyrum pernix K1]]
	[[Category: Large Structures]]		[[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: Complex with l-cysteine]]~~	+
-	~~[[Category: Cysteine biosynthesis]]~~	+
-	~~[[Category: Sulfhydrylase]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 10:02, 26 February 2020

OCA — Wed, 26 Feb 2020 10:02:25 GMT

←Older revision		Revision as of 10:02, 26 February 2020
Line 1:		Line 1:

	==Crystal Structure of the O-Phosphoserine Sulfhydrylase from Aeropyrum pernix Complexed with Cysteine==		==Crystal Structure of the O-Phosphoserine Sulfhydrylase from Aeropyrum pernix Complexed with Cysteine==
-	<StructureSection load='5b36' size='340' side='right' caption='[[5b36]], [[Resolution\|resolution]] 2.15Å' scene=''>	+	<StructureSection load='5b36' size='340' side='right'caption='[[5b36]], [[Resolution\|resolution]] 2.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5b36]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B36 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B36 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5b36]] 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=5B36 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B36 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5b3a\|5b3a]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5b3a\|5b3a]]</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=5b36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b36 OCA], [http://pdbe.org/5b36 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b36 RCSB], [http://www.ebi.ac.uk/pdbsum/5b36 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b36 ProSAT]</span></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=5b36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b36 OCA], [http://pdbe.org/5b36 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b36 RCSB], [http://www.ebi.ac.uk/pdbsum/5b36 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b36 ProSAT]</span></td></tr>
	</table>		</table>
Line 23:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Aerpe]]
		+	[[Category: Large Structures]]
	[[Category: Ishikawa, K]]		[[Category: Ishikawa, K]]
	[[Category: Kataoka, M]]		[[Category: Kataoka, M]]

OCA at 06:31, 26 July 2016

OCA — Tue, 26 Jul 2016 06:31:16 GMT

←Older revision		Revision as of 06:31, 26 July 2016
Line 6:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5b3a\|5b3a]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5b3a\|5b3a]]</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=5b36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b36 OCA], [http://pdbe.org/5b36 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b36 RCSB], [http://www.ebi.ac.uk/pdbsum/5b36 PDBsum]</span></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=5b36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b36 OCA], [http://pdbe.org/5b36 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b36 RCSB], [http://www.ebi.ac.uk/pdbsum/5b36 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b36 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 12:		Line 12:
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
-	L-~~Cysteine is synthesized~~ from O-~~acetyl~~-L-serine (~~OAS~~) and sulfide ~~by O-acetylserine sulfhydrylase (OASS; EC 2~~.~~5.1.47) in plants and bacteria. O~~-~~phosphoserine sulfhydrylase (~~OPSS~~; EC 2.5.1.65) is a novel enzyme~~ from ~~the~~ hyperthermophilic ~~aerobic~~ archaeon Aeropyrum pernix K1 (~~2003~~)~~. OPSS can use OAS or O-phospho-L-serine~~ (~~OPS~~) ~~to synthesize L~~-cysteine. ~~To elucidate the mechanism of the substrate specificity of OPSS, we analyzed three-dimensional structures~~ of the active site of the ~~enzyme~~. The ~~active~~-~~site lysine~~ (~~K127~~) of ~~OPSS forms an internal Schiff base with pyridoxal 5'-phosphate~~. ~~Therefore, crystals~~ of the ~~complexes formed by the K127A mutant with the external Schiff base~~ of ~~pyridoxal 5'-phosphate with either~~ OPS or OAS ~~were prepared and examined~~ by X-~~ray diffraction analysis~~. ~~In contrast to that observed for OASS, no significant difference~~ was ~~seen~~ in the ~~overall structure between~~ the ~~free and complexed forms of OPSS~~. ~~The side chains of T152, S153~~, and ~~Q224 interacted with the carboxylate of the substrates~~, ~~as a previous study has suggested. The side chain of R297 has been proposed~~ to ~~recognize~~ the ~~phosphate group~~ of ~~OPS. Surprisingly, however,~~ the ~~position of R297 was significantly unchanged~~ in the ~~complex of the OPSS K127A~~ mutant ~~with the external Schiff base~~, ~~allowing enough space for an interaction with OPS. The positively charged environment around~~ the entrance of the ~~active site including S153 and R297 is~~ important ~~for accepting negatively charged substrates such as OPS~~.	+	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.

-	~~Structural analysis~~ of ~~the substrate recognition mechanism~~ in O-phosphoserine sulfhydrylase from ~~the hyperthermophilic archaeon~~ Aeropyrum pernix K1.,~~Nakamura T, Kawai Y~~, Kunimoto K, ~~Iwasaki~~ Y~~, Nishii K~~, Kataoka M, Ishikawa K ~~J Mol Biol. 2012 Sep 7;422(1):33-44~~. ~~Epub 2012 May 11~~. PMID:~~22580223~~<ref>PMID:~~22580223~~</ref>	+	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<ref>PMID:27377295</ref>

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

OCA at 03:46, 11 May 2016

OCA — Wed, 11 May 2016 03:46:26 GMT

←Older revision		Revision as of 03:46, 11 May 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5b36 is ~~ON HOLD~~	+	==Crystal Structure of the O-Phosphoserine Sulfhydrylase from Aeropyrum pernix Complexed with Cysteine==
		+	<StructureSection load='5b36' size='340' side='right' caption='[[5b36]], [[Resolution\|resolution]] 2.15Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5b36]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B36 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B36 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5b3a\|5b3a]]</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=5b36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b36 OCA], [http://pdbe.org/5b36 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b36 RCSB], [http://www.ebi.ac.uk/pdbsum/5b36 PDBsum]</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>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	L-Cysteine is synthesized from O-acetyl-L-serine (OAS) and sulfide by O-acetylserine sulfhydrylase (OASS; EC 2.5.1.47) in plants and bacteria. O-phosphoserine sulfhydrylase (OPSS; EC 2.5.1.65) is a novel enzyme from the hyperthermophilic aerobic archaeon Aeropyrum pernix K1 (2003). OPSS can use OAS or O-phospho-L-serine (OPS) to synthesize L-cysteine. To elucidate the mechanism of the substrate specificity of OPSS, we analyzed three-dimensional structures of the active site of the enzyme. The active-site lysine (K127) of OPSS forms an internal Schiff base with pyridoxal 5'-phosphate. Therefore, crystals of the complexes formed by the K127A mutant with the external Schiff base of pyridoxal 5'-phosphate with either OPS or OAS were prepared and examined by X-ray diffraction analysis. In contrast to that observed for OASS, no significant difference was seen in the overall structure between the free and complexed forms of OPSS. The side chains of T152, S153, and Q224 interacted with the carboxylate of the substrates, as a previous study has suggested. The side chain of R297 has been proposed to recognize the phosphate group of OPS. Surprisingly, however, the position of R297 was significantly unchanged in the complex of the OPSS K127A mutant with the external Schiff base, allowing enough space for an interaction with OPS. The positively charged environment around the entrance of the active site including S153 and R297 is important for accepting negatively charged substrates such as OPS.

-	~~Authors: Nakamura~~, T~~., Takeda, E.~~, Kawai, Y., ~~Kataoka~~, M., Ishikawa, K.	+	Structural analysis of the substrate recognition mechanism in O-phosphoserine sulfhydrylase from the hyperthermophilic archaeon Aeropyrum pernix K1.,Nakamura T, Kawai Y, Kunimoto K, Iwasaki Y, Nishii K, Kataoka M, Ishikawa K J Mol Biol. 2012 Sep 7;422(1):33-44. Epub 2012 May 11. PMID:22580223<ref>PMID:22580223</ref>

-	~~Description: Crystal Structure~~ of the ~~O-Phosphoserine Sulfhydrylase from Aeropyrum pernix Complexed with Cysteine~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[Category: Unreleased Structures]]~~	+	</div>
-	~~[[Category~~: ~~Kawai, Y]]~~	+	<div class="pdbe-citations 5b36" style="background-color:#fffaf0;"></div>
-	~~[[Category: Takeda, E]]~~	+	== References ==
-	~~[[Category: Nakamura, T]]~~	+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Ishikawa, K]]		[[Category: Ishikawa, K]]
	[[Category: Kataoka, M]]		[[Category: Kataoka, M]]
		+	[[Category: Kawai, Y]]
		+	[[Category: Nakamura, T]]
		+	[[Category: Takeda, E]]
		+	[[Category: Complex with l-cysteine]]
		+	[[Category: Cysteine biosynthesis]]
		+	[[Category: Sulfhydrylase]]
		+	[[Category: Transferase]]

OCA: Protected "5b36" [edit=sysop:move=sysop]

OCA — Sat, 20 Feb 2016 21:12:58 GMT

Protected "5b36" [edit=sysop:move=sysop]

←Older revision

Revision as of 21:12, 20 February 2016

OCA: New page: '''Unreleased structure''' The entry 5b36 is ON HOLD Authors: Nakamura, T., Takeda, E., Kawai, Y., Kataoka, M., Ishikawa, K. Description: Crystal Structure of the O-Phosphoserine Sulfh...

OCA — Sat, 20 Feb 2016 21:12:56 GMT

New page: '''Unreleased structure''' The entry 5b36 is ON HOLD Authors: Nakamura, T., Takeda, E., Kawai, Y., Kataoka, M., Ishikawa, K. Description: Crystal Structure of the O-Phosphoserine Sulfh...

New page

'''Unreleased structure'''

The entry 5b36 is ON HOLD

Authors: Nakamura, T., Takeda, E., Kawai, Y., Kataoka, M., Ishikawa, K.

Description: Crystal Structure of the O-Phosphoserine Sulfhydrylase from Aeropyrum pernix Complexed with Cysteine
[[Category: Unreleased Structures]]
[[Category: Kawai, Y]]
[[Category: Takeda, E]]
[[Category: Nakamura, T]]
[[Category: Ishikawa, K]]
[[Category: Kataoka, M]]