Proline utilization A: Difference between revisions

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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)''' 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 ==
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>


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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


**[[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 />
**[[5ur2]] - PutA + FAD derivative - ''Bdellovibrio bacteriovorus''<br />
**[[6ufp]], [[6vz9]] – SmPutA (mutant) + FAD ''Sinorhizobium melioli''<br />


*PutA complex
*PutA complex
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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 />
**[[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 />
}}
}}


Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman