8jfi - Revision history

OCA at 11:11, 22 November 2023

2023-11-22T11:11:13Z

←Older revision		Revision as of 11:11, 22 November 2023
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 8jfi is ~~ON HOLD until Paper~~ Publication	+	==Crystal structure of 3-oxoacyl-ACP reductase FabG in complex with NADP+ and 3-keto-hexanoyl-ACP from Helicobacter pylori==
		+	<StructureSection load='8jfi' size='340' side='right'caption='[[8jfi]], [[Resolution\|resolution]] 2.38Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[8jfi]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8JFI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8JFI 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]] 2.38Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=UHC:~{S}-[2-[3-[[(2~{S})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butanoyl]amino]propanoylamino]ethyl]+3-oxidanylideneoctanethioate'>UHC</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=8jfi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8jfi OCA], [https://pdbe.org/8jfi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8jfi RCSB], [https://www.ebi.ac.uk/pdbsum/8jfi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8jfi ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/G2M827_HELPX G2M827_HELPX] Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.[RuleBase:RU366074]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The short-chain dehydrogenase/reductase (SDR) superfamily members acyl-ACP reductases FabG and FabI are indispensable core enzymatic modules and catalytic orientation controllers in type-II fatty acid biosynthesis. Herein, we report their distinct substrate allosteric recognition and enantioselective reduction mechanisms. FabG achieves allosteric regulation of ACP and NADPH through ACP binding across two adjacent FabG monomers, while FabI follows an irreversible compulsory order of substrate binding in that NADH binding must precede that of ACP on a discrete FabI monomer. Moreover, FabG and FabI utilize a backdoor residue Phe187 or a "rheostat" alpha8 helix for acyl chain length selection, and their corresponding triad residues Ser142 or Tyr145 recognize the keto- or enoyl-acyl substrates, respectively, facilitating initiation of nucleophilic attack by NAD(P)H. The other two triad residues (Tyr and Lys) mediate subsequent proton transfer and (R)-3-hydroxyacyl- or saturated acyl-ACP production.

-	~~Authors~~:	+	The Molecular Basis of Catalysis by SDR Family Members Ketoacyl-ACP Reductase FabG and Enoyl-ACP Reductase FabI in Type-II Fatty Acid Biosynthesis.,Zhou J, Zhang L, Wang Y, Song W, Huang Y, Mu Y, Schmitz W, Zhang SY, Lin H, Chen HZ, Ye F, Zhang L Angew Chem Int Ed Engl. 2023 Nov 13;62(46):e202313109. doi: , 10.1002/anie.202313109. Epub 2023 Oct 12. PMID:37779101<ref>PMID:37779101</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 8jfi" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Helicobacter pylori]]
		+	[[Category: Large Structures]]
		+	[[Category: Zhang L]]
		+	[[Category: Zhou JS]]

OCA: Replacing page with ''''Unreleased structure''' The entry 8jfi is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures'

2023-11-22T05:33:06Z

Replacing page with ''''Unreleased structure''' The entry 8jfi is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures'

←Older revision		Revision as of 05:33, 22 November 2023
Line 1:		Line 1:
		+	'''Unreleased structure'''

-	~~==Crystal structure of 3-oxoacyl-ACP reductase FabG in complex with NADP+ and 3-keto-hexanoyl-ACP from Helicobacter pylori==~~	+	The entry 8jfi is ON HOLD until Paper Publication
-	~~<StructureSection load='~~8jfi~~' size='340' side='right'caption='[[8jfi]], [[Resolution\|resolution]] 2.38Å' scene=''>~~	+
-	~~== Structural highlights ==~~	+
-	~~<table><tr><td colspan='2'>[[8jfi]]~~ is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8JFI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8JFI 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]] 2.38Å</td></tr>~~	+
-	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=UHC:~{S}-[2-[3-[[(2~{S})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butanoyl]amino]propanoylamino]ethyl]+3-oxidanylideneoctanethioate'>UHC</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=8jfi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8jfi OCA], [https://pdbe.org/8jfi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8jfi RCSB], [https://www.ebi.ac.uk/pdbsum/8jfi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8jfi ProSAT]</span></td></tr>	+
-	~~</table>~~	+
-	~~== Function ==~~	+
-	[https://www.uniprot.org/uniprot/G2M827_HELPX G2M827_HELPX] Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.[RuleBase:RU366074]	+
-	~~<div style="background-color:#fffaf0;">~~	+
-	== Publication ~~Abstract from PubMed ==~~	+
-	The short-chain dehydrogenase/reductase (SDR) superfamily members acyl-ACP reductases FabG and FabI are indispensable core enzymatic modules and catalytic orientation controllers in type-II fatty acid biosynthesis. Herein, we report their distinct substrate allosteric recognition and enantioselective reduction mechanisms. FabG achieves allosteric regulation of ACP and NADPH through ACP binding across two adjacent FabG monomers, while FabI follows an irreversible compulsory order of substrate binding in that NADH binding must precede that of ACP on a discrete FabI monomer. Moreover, FabG and FabI utilize a backdoor residue Phe187 or a "rheostat" alpha8 helix for acyl chain length selection, and their corresponding triad residues Ser142 or Tyr145 recognize the keto- or enoyl-acyl substrates, respectively, facilitating initiation of nucleophilic attack by NAD(P)H. The other two triad residues (Tyr and Lys) mediate subsequent proton transfer and (R)-3-hydroxyacyl- or saturated acyl-ACP production.	+

-	The Molecular Basis of Catalysis by SDR Family Members Ketoacyl-ACP Reductase FabG and Enoyl-ACP Reductase FabI in Type-II Fatty Acid Biosynthesis.,Zhou J, Zhang L, Wang Y, Song W, Huang Y, Mu Y, Schmitz W, Zhang SY, Lin H, Chen HZ, Ye F, Zhang L Angew Chem Int Ed Engl. 2023 Nov 13;62(46):~~e202313109. doi: , 10.1002/anie.202313109. Epub 2023 Oct 12. PMID:37779101<ref>PMID:37779101</ref>~~	+	Authors:

-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+	Description:
-	~~</div>~~	+	[[Category: Unreleased Structures]]
-	~~<div class="pdbe-citations 8jfi" style="background-color~~:~~#fffaf0;"></div>~~	+
-	~~== References ==~~	+
-	~~<references/>~~	+
-	~~__TOC__~~	+
-	~~</StructureSection>~~	+
-	[[Category: ~~Helicobacter pylori]]~~	+
-	~~[[Category: Large~~ Structures]]	+
-	~~[[Category: Zhang L]]~~	+
-	~~[[Category: Zhou JS~~]]	+

OCA at 07:36, 15 November 2023

2023-11-15T07:36:48Z

←Older revision		Revision as of 07:36, 15 November 2023
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 8jfi is ~~ON HOLD until Paper~~ Publication	+	==Crystal structure of 3-oxoacyl-ACP reductase FabG in complex with NADP+ and 3-keto-hexanoyl-ACP from Helicobacter pylori==
		+	<StructureSection load='8jfi' size='340' side='right'caption='[[8jfi]], [[Resolution\|resolution]] 2.38Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[8jfi]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8JFI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8JFI 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]] 2.38Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=UHC:~{S}-[2-[3-[[(2~{S})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butanoyl]amino]propanoylamino]ethyl]+3-oxidanylideneoctanethioate'>UHC</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=8jfi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8jfi OCA], [https://pdbe.org/8jfi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8jfi RCSB], [https://www.ebi.ac.uk/pdbsum/8jfi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8jfi ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/G2M827_HELPX G2M827_HELPX] Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.[RuleBase:RU366074]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The short-chain dehydrogenase/reductase (SDR) superfamily members acyl-ACP reductases FabG and FabI are indispensable core enzymatic modules and catalytic orientation controllers in type-II fatty acid biosynthesis. Herein, we report their distinct substrate allosteric recognition and enantioselective reduction mechanisms. FabG achieves allosteric regulation of ACP and NADPH through ACP binding across two adjacent FabG monomers, while FabI follows an irreversible compulsory order of substrate binding in that NADH binding must precede that of ACP on a discrete FabI monomer. Moreover, FabG and FabI utilize a backdoor residue Phe187 or a "rheostat" alpha8 helix for acyl chain length selection, and their corresponding triad residues Ser142 or Tyr145 recognize the keto- or enoyl-acyl substrates, respectively, facilitating initiation of nucleophilic attack by NAD(P)H. The other two triad residues (Tyr and Lys) mediate subsequent proton transfer and (R)-3-hydroxyacyl- or saturated acyl-ACP production.

-	~~Authors~~:	+	The Molecular Basis of Catalysis by SDR Family Members Ketoacyl-ACP Reductase FabG and Enoyl-ACP Reductase FabI in Type-II Fatty Acid Biosynthesis.,Zhou J, Zhang L, Wang Y, Song W, Huang Y, Mu Y, Schmitz W, Zhang SY, Lin H, Chen HZ, Ye F, Zhang L Angew Chem Int Ed Engl. 2023 Nov 13;62(46):e202313109. doi: , 10.1002/anie.202313109. Epub 2023 Oct 12. PMID:37779101<ref>PMID:37779101</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 8jfi" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Helicobacter pylori]]
		+	[[Category: Large Structures]]
		+	[[Category: Zhang L]]
		+	[[Category: Zhou JS]]

OCA at 03:54, 5 July 2023

2023-07-05T03:54:59Z

←Older revision		Revision as of 03:54, 5 July 2023
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 8jfi is ON HOLD	+	The entry 8jfi is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "8jfi" [edit=sysop:move=sysop]

2023-05-25T02:29:52Z

Protected "8jfi" [edit=sysop:move=sysop]

←Older revision

Revision as of 02:29, 25 May 2023

OCA: New page: '''Unreleased structure''' The entry 8jfi is ON HOLD Authors: Description: Category: Unreleased Structures

2023-05-25T02:29:51Z

New page: '''Unreleased structure''' The entry 8jfi is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 8jfi is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]