Proline utilization A - Revision history

Michal Harel at 08:52, 19 July 2026

2026-07-19T08:52:04Z

← Older revision		Revision as of 08:52, 19 July 2026
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	**[[5ur2]] - PutA + FAD derivative + inhibitor - ''Bdellovibrio bacteriovorus''<br />		**[[5ur2]] - PutA + FAD derivative + inhibitor - ''Bdellovibrio bacteriovorus''<br />
	**[[6x9a]], [[6x9b]], [[6x9c]], [[6x9d]] – SmPutA + FAD + proline derivative <br />		**[[6x9a]], [[6x9b]], [[6x9c]], [[6x9d]] – SmPutA + FAD + proline derivative <br />
	**[[6x99]] – SmPutA + FAD + Glu derivative <br />		**[[6x99]], [[9bbo]] – SmPutA + FAD + Glu derivative <br />
			**[[9e5w]] – SmPutA + NAD + propargylglycine <br />
			**[[9c8c]] – SmPutA + NAD + FAD + allylgylglycine <br />
			**[[9c35]], [[9c36]] – SmPutA + NAD + FAD + Glu derivative<br />
			**[[9c34]] – SmPutA + NAD + FAD + Pro<br />
			**[[9dl8]], [[9dl9]], [[9e0a]], [[9e0b]], [[9e0c]], [[9e0d]], [[9e0e]] – SmPutA + NAD + FAD + alcohol<br />
			**[[9dl7]] – SmPutA + NAD + FAD + urea derivative<br />
			**[[9dl2]], [[9dl3]], [[9dl6]] – SmPutA + NAD + FAD + carboxylic acid derivative<br />
			**[[9dl4]] – SmPutA + NAD + FAD + pyridinethiol<br />
			**[[9dl5]] – SmPutA + NAD + FAD + indanone derivative<br />
	**[[7my9]], [[7mya]], [[7myb]], [[7myc]] – SmPutA + FAD + dithiolane <br />		**[[7my9]], [[7mya]], [[7myb]], [[7myc]] – SmPutA + FAD + dithiolane <br />
	**[[6bsn]] – BdPutA + FAD + proline<br />		**[[6bsn]] – BdPutA + FAD + proline<br />

Michal Harel at 10:15, 1 February 2022

2022-02-01T10:15:40Z

← Older revision		Revision as of 10:15, 1 February 2022
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	**[[4nm9]] – GsPutA + FAD – ''Geobacter sulfurreducens'' <br />		**[[4nm9]] – GsPutA + FAD – ''Geobacter sulfurreducens'' <br />
			**[[7na0]] – GsPutA (mutant) + FAD <br />
	**[[4nma]] – GsPutA + FAD + tetrahydrofuran derivative <br />		**[[4nma]] – GsPutA + FAD + tetrahydrofuran derivative <br />
	**[[2gpe]] – EcPutA DNA-binding domain <br />		**[[2gpe]] – EcPutA DNA-binding domain <br />
	**[[2ay0]] – EcPutA DNA-binding domain (mutant)<br />		**[[2ay0]] – EcPutA DNA-binding domain (mutant)<br />
	**[[4q71]], [[4q72]], [[4q73]] – ~~PutA~~ (mutant) + FAD – ''Bradyrhizobium diazoefficiens''<br />		**[[4q71]], [[4q72]], [[4q73]] – BdPutA (mutant) + FAD – ''Bradyrhizobium diazoefficiens''<br />
	**[[4h6r]] – DrPutA + FAD – ''Deinococcus radiodurans''<br />		**[[4h6r]] – DrPutA + FAD – ''Deinococcus radiodurans''<br />
	**[[2gpe]] - EcPutA DNA-binding domain - ''Escherichia coli''<br />		**[[2gpe]] - EcPutA DNA-binding domain - ''Escherichia coli''<br />
	**[[2jxg]], [[2jxh]] - PpPutA DNA-binding domain - ''Pseudomonas putida'' - NMR<br />		**[[2jxg]], [[2jxh]] - PpPutA DNA-binding domain - ''Pseudomonas putida'' - NMR<br />
			**[[6ufp]], [[6vz9]] – SmPutA (mutant) + FAD – ''Sinorhizobium melioli''<br />

	*PutA complex		*PutA complex

	**[[6bsn]] – hPutA + FAD derivative + Pro - human<br />
	**[[4nmb]] – GsPutA + FAD + lactate <br />		**[[4nmb]] – GsPutA + FAD + lactate <br />
	**[[4nmc]] – GsPutA + FAD + zwittergent <br />		**[[4nmc]] – GsPutA + FAD + zwittergent <br />
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	**[[2jxi]] - PpPutA DNA-binding domain + DNA<br />		**[[2jxi]] - PpPutA DNA-binding domain + DNA<br />
	**[[5ur2]] - PutA + FAD derivative + inhibitor - ''Bdellovibrio bacteriovorus''<br />		**[[5ur2]] - PutA + FAD derivative + inhibitor - ''Bdellovibrio bacteriovorus''<br />
			**[[6x9a]], [[6x9b]], [[6x9c]], [[6x9d]] – SmPutA + FAD + proline derivative <br />
			**[[6x99]] – SmPutA + FAD + Glu derivative <br />
			**[[7my9]], [[7mya]], [[7myb]], [[7myc]] – SmPutA + FAD + dithiolane <br />
			**[[6bsn]] – BdPutA + FAD + proline<br />
	}}		}}

Michal Harel at 07:52, 7 October 2020

2020-10-07T07:52:01Z

← Older revision		Revision as of 07:52, 7 October 2020
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	<StructureSection load='' size='350' side='right' caption='E. coli PutA proline dehydrogenase domain with cofactor FAD complex with hydroxyproline (PDB code [[3e2q]])' scene='70/706260/Cv/1'>		<StructureSection load='' size='350' side='right' caption='E. coli PutA proline dehydrogenase domain with cofactor FAD complex with hydroxyproline (PDB code [[3e2q]])' scene='70/706260/Cv/1'>
	== Function ==		== Function ==
	'''Proline utilization A (PutA)''' is a bifunctional flavoprotein which acts as a transcriptional repressor of the put regulon or as a membrane-bound enzyme which catalyzes the oxidation of proline to glutamate. PutA domains include the DNA-binding domain (PRODH), the FAD-dependent proline dehydrogenase domain and the D-pyrroline-5-carboxylate dehydrogenase domain. The binding of proline to the PRODH active site and subsequent reduction of FAD causes a conformation change in PutA and enhance its membrane affinity. As a membrane-bound protein PutA switches from its repressor activity to its enzymatic role<ref>PMID:19994913</ref>.		'''Proline utilization A (PutA)''' or '''bifunctional protein PutA''' is a bifunctional flavoprotein which acts as a transcriptional repressor of the put regulon or as a membrane-bound enzyme which catalyzes the oxidation of proline to glutamate. PutA domains include the DNA-binding domain (PRODH), the FAD-dependent proline dehydrogenase domain and the D-pyrroline-5-carboxylate dehydrogenase domain. The binding of proline to the PRODH active site and subsequent reduction of FAD causes a conformation change in PutA and enhance its membrane affinity. As a membrane-bound protein PutA switches from its repressor activity to its enzymatic role<ref>PMID:19994913</ref>.

	== Structural highlights ==		== Structural highlights ==
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	Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}		Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
	{{#tree:id=OrganizedByTopic\|openlevels=0\|		{{#tree:id=OrganizedByTopic\|openlevels=0\|

	*PutA		*PutA

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	**[[2gpe]] - EcPutA DNA-binding domain - ''Escherichia coli''<br />		**[[2gpe]] - EcPutA DNA-binding domain - ''Escherichia coli''<br />
	**[[2jxg]], [[2jxh]] - PpPutA DNA-binding domain - ''Pseudomonas putida'' - NMR<br />		**[[2jxg]], [[2jxh]] - PpPutA DNA-binding domain - ''Pseudomonas putida'' - NMR<br />
	**[[5ur2]] - PutA + FAD derivative - ''Bdellovibrio bacteriovorus''<br />

	*PutA complex		*PutA complex

			**[[6bsn]] – hPutA + FAD derivative + Pro - human<br />
	**[[4nmb]] – GsPutA + FAD + lactate <br />		**[[4nmb]] – GsPutA + FAD + lactate <br />
	**[[4nmc]] – GsPutA + FAD + zwittergent <br />		**[[4nmc]] – GsPutA + FAD + zwittergent <br />
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	**[[3haz]] - PutA + FAD + NAD - ''Bradyrhyzobium japonicum''<br />		**[[3haz]] - PutA + FAD + NAD - ''Bradyrhyzobium japonicum''<br />
	**[[5ux5]] - PutA + FAD + NAD - ''Corynebacterium freiburgense''<br />		**[[5ux5]] - PutA + FAD + NAD - ''Corynebacterium freiburgense''<br />
	**[[5kf6]], [[5kf7]] - PutA + FAD + NAD + THF - ''Sinorhizobium meliloti''<br />		**[[5kf6]], [[5kf7]], [[6ufp]], [[6vz9]] - PutA + FAD + NAD + THF - ''Sinorhizobium meliloti''<br />
	**[[2jxi]] - PpPutA DNA-binding domain + DNA<br />		**[[2jxi]] - PpPutA DNA-binding domain + DNA<br />
			**[[5ur2]] - PutA + FAD derivative + inhibitor - ''Bdellovibrio bacteriovorus''<br />
	}}		}}

Michal Harel at 08:08, 28 November 2019

2019-11-28T08:08:11Z

← Older revision		Revision as of 08:08, 28 November 2019
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	**[[5kf6]], [[5kf7]] - PutA + FAD + NAD + THF - ''Sinorhizobium meliloti''<br />		**[[5kf6]], [[5kf7]] - PutA + FAD + NAD + THF - ''Sinorhizobium meliloti''<br />
	**[[2jxi]] - PpPutA DNA-binding domain + DNA<br />		**[[2jxi]] - PpPutA DNA-binding domain + DNA<br />

	}}		}}

Alexander Berchansky at 13:16, 14 August 2019

2019-08-14T13:16:03Z

← Older revision		Revision as of 13:16, 14 August 2019
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	== Structural highlights ==		== Structural highlights ==
	The <scene name='70/706260/Cv/3'>active site residue Tyr540 helps in substrate preference for proline over hydroxyproline</scene>. Water molecules shown as red spheres. The [[3e2q]] structure displayed here contains the <scene name='70/706260/Cv/4'>Tyr540Ser mutant</scene><ref>PMID:19140736</ref>.		The <scene name='70/706260/Cv/5'>active site residue Tyr540 helps in substrate preference for proline over hydroxyproline</scene>. Water molecules are shown as red spheres. The [[3e2q]] structure displayed here contains the <scene name='70/706260/Cv/6'>Tyr540Ser mutant</scene><ref>PMID:19140736</ref>.
	</StructureSection>		</StructureSection>

Michal Harel at 10:27, 26 August 2018

2018-08-26T10:27:03Z

← Older revision		Revision as of 10:27, 26 August 2018
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	<StructureSection load='' size='~~450~~' side='right' caption='E. coli PutA proline dehydrogenase domain with cofactor FAD complex with hydroxyproline (PDB code [[3e2q]])' scene='70/706260/Cv/1'>		<StructureSection load='' size='350' side='right' caption='E. coli PutA proline dehydrogenase domain with cofactor FAD complex with hydroxyproline (PDB code [[3e2q]])' scene='70/706260/Cv/1'>
	== Function ==		== Function ==
	'''Proline utilization A (PutA)''' is a bifunctional flavoprotein which acts as a transcriptional repressor of the put regulon or as a membrane-bound enzyme which catalyzes the oxidation of proline to glutamate. PutA domains include the DNA-binding domain (PRODH), the FAD-dependent proline dehydrogenase domain and the D-pyrroline-5-carboxylate dehydrogenase domain. The binding of proline to the PRODH active site and subsequent reduction of FAD causes a conformation change in PutA and enhance its membrane affinity. As a membrane-bound protein PutA switches from its repressor activity to its enzymatic role<ref>PMID:19994913</ref>.		'''Proline utilization A (PutA)''' is a bifunctional flavoprotein which acts as a transcriptional repressor of the put regulon or as a membrane-bound enzyme which catalyzes the oxidation of proline to glutamate. PutA domains include the DNA-binding domain (PRODH), the FAD-dependent proline dehydrogenase domain and the D-pyrroline-5-carboxylate dehydrogenase domain. The binding of proline to the PRODH active site and subsequent reduction of FAD causes a conformation change in PutA and enhance its membrane affinity. As a membrane-bound protein PutA switches from its repressor activity to its enzymatic role<ref>PMID:19994913</ref>.

Michal Harel at 13:18, 23 October 2017

2017-10-23T13:18:13Z

← Older revision		Revision as of 13:18, 23 October 2017
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	== References ==		== References ==
	<references/>		<references/>
			[[Category:Topic Page]]

Joel L. Sussman at 12:54, 21 October 2017

2017-10-21T12:54:00Z

← Older revision		Revision as of 12:54, 21 October 2017
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	<StructureSection load='~~3e2q~~' size='450' side='right' caption='E. coli PutA proline dehydrogenase domain with cofactor FAD complex with hydroxyproline (PDB code [[3e2q]])' scene='70/706260/Cv/1'>		<StructureSection load='' size='450' side='right' caption='E. coli PutA proline dehydrogenase domain with cofactor FAD complex with hydroxyproline (PDB code [[3e2q]])' scene='70/706260/Cv/1'>
	== Function ==		== Function ==
	'''Proline utilization A (PutA)''' is a bifunctional flavoprotein which acts as a transcriptional repressor of the put regulon or as a membrane-bound enzyme which catalyzes the oxidation of proline to glutamate. PutA domains include the DNA-binding domain (PRODH), the FAD-dependent proline dehydrogenase domain and the D-pyrroline-5-carboxylate dehydrogenase domain. The binding of proline to the PRODH active site and subsequent reduction of FAD causes a conformation change in PutA and enhance its membrane affinity. As a membrane-bound protein PutA switches from its repressor activity to its enzymatic role<ref>PMID:19994913</ref>.		'''Proline utilization A (PutA)''' is a bifunctional flavoprotein which acts as a transcriptional repressor of the put regulon or as a membrane-bound enzyme which catalyzes the oxidation of proline to glutamate. PutA domains include the DNA-binding domain (PRODH), the FAD-dependent proline dehydrogenase domain and the D-pyrroline-5-carboxylate dehydrogenase domain. The binding of proline to the PRODH active site and subsequent reduction of FAD causes a conformation change in PutA and enhance its membrane affinity. As a membrane-bound protein PutA switches from its repressor activity to its enzymatic role<ref>PMID:19994913</ref>.

Michal Harel at 18:37, 19 September 2017

2017-09-19T18:37:01Z

← Older revision		Revision as of 18:37, 19 September 2017
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	**[[4q71]], [[4q72]], [[4q73]] – PutA (mutant) + FAD – ''Bradyrhizobium diazoefficiens''<br />		**[[4q71]], [[4q72]], [[4q73]] – PutA (mutant) + FAD – ''Bradyrhizobium diazoefficiens''<br />
	**[[4h6r]] – DrPutA + FAD – ''Deinococcus radiodurans''<br />		**[[4h6r]] – DrPutA + FAD – ''Deinococcus radiodurans''<br />
			**[[2gpe]] - EcPutA DNA-binding domain - ''Escherichia coli''<br />
			**[[2jxg]], [[2jxh]] - PpPutA DNA-binding domain - ''Pseudomonas putida'' - NMR<br />
			**[[5ur2]] - PutA + FAD derivative - ''Bdellovibrio bacteriovorus''<br />

	*PutA complex		*PutA complex
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	**[[4nme]] – GsPutA + FAD + propargylglycine <br />		**[[4nme]] – GsPutA + FAD + propargylglycine <br />
	**[[4nmf]] – GsPutA + FAD derivative + menadione bisulfite<br />		**[[4nmf]] – GsPutA + FAD derivative + menadione bisulfite<br />
	**[[1tiw]] – EcPutA PRODH domain + FAD + tetrahydrofuran derivative ~~– ''Escherichia coli''~~<br />		**[[1tiw]] – EcPutA PRODH domain + FAD + tetrahydrofuran derivative <br />
	**[[3e2r]], [[4jny]], [[4jnz]] – EcPutA PRODH domain (mutant) + FAD + tetrahydrofuran derivative <br />		**[[3e2r]], [[4jny]], [[4jnz]] – EcPutA PRODH domain (mutant) + FAD + tetrahydrofuran derivative <br />
	**[[1tj0]], [[1tj1]] – EcPutA PRODH domain + FAD + lactate<br />		**[[1tj0]], [[1tj1]] – EcPutA PRODH domain + FAD + lactate<br />
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	**[[4o8a]] – EcPutA DNA-binding + PRODH domains + FAD <br />		**[[4o8a]] – EcPutA DNA-binding + PRODH domains + FAD <br />
	**[[4h6q]] – DrPutA + FAD + THF <br />		**[[4h6q]] – DrPutA + FAD + THF <br />
			**[[3haz]] - PutA + FAD + NAD - ''Bradyrhyzobium japonicum''<br />
			**[[5ux5]] - PutA + FAD + NAD - ''Corynebacterium freiburgense''<br />
			**[[5kf6]], [[5kf7]] - PutA + FAD + NAD + THF - ''Sinorhizobium meliloti''<br />
			**[[2jxi]] - PpPutA DNA-binding domain + DNA<br />
	}}		}}

	== References ==		== References ==
	<references/>		<references/>

Alexander Berchansky at 10:17, 28 July 2016

2016-07-28T10:17:08Z

← Older revision		Revision as of 10:17, 28 July 2016
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	== Structural highlights ==		== Structural highlights ==
	The active site residue Tyr540 helps in substrate preference for proline over hydroxyproline. The [[3e2q]] structure displayed here contains the Tyr540Ser mutant<ref>PMID:19140736</ref>.		The <scene name='70/706260/Cv/3'>active site residue Tyr540 helps in substrate preference for proline over hydroxyproline</scene>. Water molecules shown as red spheres. The [[3e2q]] structure displayed here contains the <scene name='70/706260/Cv/4'>Tyr540Ser mutant</scene><ref>PMID:19140736</ref>.
	</StructureSection>		</StructureSection>