Proline utilization A

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<StructureSection load='3e2q' size='340' side='right' caption='E. coli PutA proline dehydrogenase domain with cofactor FAD complex with hydroxyproline (PDB code [[3e2q]])' scene=''>
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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'>
== Function ==
== Function ==
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'''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>.
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'''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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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>.
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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>
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*PutA
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[[4nm9]] – GsPutA + FAD – ''Geobacter sulfurreducens'' <br />
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**[[4nm9]] – GsPutA + FAD – ''Geobacter sulfurreducens'' <br />
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[[4nma]] – GsPutA + FAD + tetrahydrofuran derivative <br />
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**[[7na0]] – GsPutA (mutant) + FAD <br />
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[[4nmb]] – GsPutA + FAD + lactate <br />
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**[[4nma]] – GsPutA + FAD + tetrahydrofuran derivative <br />
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[[4nmc]] – GsPutA + FAD + zwittergent <br />
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**[[2gpe]] – EcPutA DNA-binding domain <br />
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[[4nmd]] – GsPutA + FAD + dithionite <br />
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**[[2ay0]] – EcPutA DNA-binding domain (mutant)<br />
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[[4nme]] – GsPutA + FAD + propargylglycine <br />
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**[[4q71]], [[4q72]], [[4q73]] – BdPutA (mutant) + FAD – ''Bradyrhizobium diazoefficiens''<br />
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[[4nmf]] – GsPutA + FAD derivative + menadione bisulfite<br />
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**[[4h6r]] – DrPutA + FAD – ''Deinococcus radiodurans''<br />
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[[1tiw]] – EcPutA PRODH domain + FAD + tetrahydrofuran derivative – ''Escherichia coli''<br />
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**[[2gpe]] - EcPutA DNA-binding domain - ''Escherichia coli''<br />
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[[3e2r]], [[4jny]], [[4jnz]] – EcPutA PRODH domain (mutant) + FAD + tetrahydrofuran derivative <br />
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**[[2jxg]], [[2jxh]] - PpPutA DNA-binding domain - ''Pseudomonas putida'' - NMR<br />
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[[1tj0]], [[1tj1]] – EcPutA PRODH domain + FAD + lactate<br />
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**[[6ufp]], [[6vz9]] – SmPutA (mutant) + FAD – ''Sinorhizobium melioli''<br />
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[[1tj2]] – EcPutA PRODH domain + FAD + acetate<br />
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[[2fzn]] – EcPutA PRODH domain + FAD + proline<br />
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*PutA complex
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[[3e2q]], [[3e2s]] – EcPutA PRODH domain (mutant) + FAD + proline derivative<br />
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[[2fzm]] – EcPutA PRODH domain + FAD + SO2<br />
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**[[4nmb]] – GsPutA + FAD + lactate <br />
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[[3itg]] – EcPutA PRODH domain + FAD + propargylglycine <br />
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**[[4nmc]] – GsPutA + FAD + zwittergent <br />
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[[2gpe]] – EcPutA DNA-binding domain <br />
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**[[4nmd]] – GsPutA + FAD + dithionite <br />
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[[2ay0]] – EcPutA DNA-binding domain (mutant)<br />
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**[[4nme]] – GsPutA + FAD + propargylglycine <br />
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[[2rbf]] – EcPutA DNA-binding domain + DNA<br />
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**[[4nmf]] – GsPutA + FAD derivative + menadione bisulfite<br />
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[[4o8a]] – EcPutA DNA-binding + PRODH domains + FAD <br />
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**[[1tiw]] – EcPutA PRODH domain + FAD + tetrahydrofuran derivative <br />
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**[[3e2r]], [[4jny]], [[4jnz]] – EcPutA PRODH domain (mutant) + FAD + tetrahydrofuran derivative <br />
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**[[1tj0]], [[1tj1]] – EcPutA PRODH domain + FAD + lactate<br />
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**[[1tj2]] – EcPutA PRODH domain + FAD + acetate<br />
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**[[2fzn]] – EcPutA PRODH domain + FAD + proline<br />
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**[[3e2q]], [[3e2s]] – EcPutA PRODH domain (mutant) + FAD + proline derivative<br />
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**[[2fzm]] – EcPutA PRODH domain + FAD + SO2<br />
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**[[3itg]] – EcPutA PRODH domain + FAD + propargylglycine <br />
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**[[2rbf]] – EcPutA DNA-binding domain + DNA<br />
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**[[4o8a]] – EcPutA DNA-binding + PRODH domains + FAD <br />
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**[[4h6q]] – DrPutA + FAD + THF <br />
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**[[3haz]] - PutA + FAD + NAD - ''Bradyrhyzobium japonicum''<br />
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**[[5ux5]] - PutA + FAD + NAD - ''Corynebacterium freiburgense''<br />
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**[[5kf6]], [[5kf7]], [[6ufp]], [[6vz9]] - PutA + FAD + NAD + THF - ''Sinorhizobium meliloti''<br />
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**[[2jxi]] - PpPutA DNA-binding domain + DNA<br />
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**[[5ur2]] - PutA + FAD derivative + inhibitor - ''Bdellovibrio bacteriovorus''<br />
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**[[6x9a]], [[6x9b]], [[6x9c]], [[6x9d]] – SmPutA + FAD + proline derivative <br />
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**[[6x99]] – SmPutA + FAD + Glu derivative <br />
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**[[7my9]], [[7mya]], [[7myb]], [[7myc]] – SmPutA + FAD + dithiolane <br />
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**[[6bsn]] – BdPutA + FAD + proline<br />
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}}
== References ==
== References ==
<references/>
<references/>
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[[Category:Topic Page]]

Current revision

E. coli PutA proline dehydrogenase domain with cofactor FAD complex with hydroxyproline (PDB code 3e2q)

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3D Structures of proline utilization A

Updated on 01-February-2022

References

  1. ↑ Srivastava D, Zhu W, Johnson WH, Whitman CP, Becker DF, Tanner JJ. The Structure of the Proline Utilization A Proline Dehydrogenase Domain Inactivated by N-Propargylglycine Provides Insight into Conformational Changes Induced by Substrate Binding and Flavin Reduction (,). Biochemistry. 2009 Dec 29. PMID:19994913 doi:10.1021/bi901717s
  2. ↑ Ostrander EL, Larson JD, Schuermann JP, Tanner JJ. A Conserved Active Site Tyrosine Residue of Proline Dehydrogenase Helps Enforce the Preference for Proline over Hydroxyproline as the Substrate (dagger) (double dagger). Biochemistry. 2009 Feb 10;48(5):951-9. PMID:19140736 doi:10.1021/bi802094k

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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