Proline utilization A: Difference between revisions
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<StructureSection load=' | <StructureSection load='3e2q' size='340' side='right' caption='E. coli PutA proline dehydrogenase domain with cofactor FAD complex with hydroxyproline (PDB code [[3e2q])' scene=''> | ||
== 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>. | ||
== 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>. | |||
</StructureSection> | </StructureSection> | ||
Revision as of 11:46, 12 July 2016
FunctionProline 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[1]. Structural highlightsThe active site residue Tyr540 helps in substrate preference for proline over hydroxyproline. The 3e2q structure displayed here contains the Tyr540Ser mutant[2]. |
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3D Structures of proline utilization A3D Structures of proline utilization A
Updated on 12-July-2016
4nm9 – GsPutA + FAD – Geobacter sulfurreducens
4nma – GsPutA + FAD + tetrahydrofuran derivative
4nmb – GsPutA + FAD + lactate
4nmc – GsPutA + FAD + zwittergent
4nmd – GsPutA + FAD + dithionite
4nme – GsPutA + FAD + propargylglycine
4nmf – GsPutA + FAD derivative + menadione bisulfite
1tiw – EcPutA PRODH domain + FAD + tetrahydrofuran derivative – Escherichia coli
3e2r, 4jny, 4jnz – EcPutA PRODH domain (mutant) + FAD + tetrahydrofuran derivative
1tj0, 1tj1 – EcPutA PRODH domain + FAD + lactate
1tj2 – EcPutA PRODH domain + FAD + acetate
2fzn – EcPutA PRODH domain + FAD + proline
3e2q, 3e2s – EcPutA PRODH domain (mutant) + FAD + proline derivative
2fzm – EcPutA PRODH domain + FAD + SO2
3itg – EcPutA PRODH domain + FAD + propargylglycine
2gpe – EcPutA DNA-binding domain
2ay0 – EcPutA DNA-binding domain (mutant)
2rbf – EcPutA DNA-binding domain + DNA
4o8a – EcPutA DNA-binding + PRODH domains + FAD
ReferencesReferences
- ↑ 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
- ↑ 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