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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> |
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Revision as of 13:16, 14 August 2019
| 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[1].
Structural highlights
The active site residue Tyr540 helps in substrate preference for proline over hydroxyproline. Water molecules are shown as red spheres. The 3e2q structure displayed here contains the Tyr540Ser mutant[2].
- ↑ 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
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3D Structures of proline utilization A
Updated on 14-August-2019
{"openlevels":0}
- PutA
- 3e2q – GsPutA + FAD – Geobacter sulfurreducens
- 4nma – GsPutA + FAD + tetrahydrofuran derivative
- 2gpe – EcPutA DNA-binding domain
- 2ay0 – EcPutA DNA-binding domain (mutant)
- 4q71, 4q72, 4q73 – PutA (mutant) + FAD – Bradyrhizobium diazoefficiens
- 4h6r – DrPutA + FAD – Deinococcus radiodurans
- 2gpe - EcPutA DNA-binding domain - Escherichia coli
- 2jxg, 2jxh - PpPutA DNA-binding domain - Pseudomonas putida - NMR
- 5ur2 - PutA + FAD derivative - Bdellovibrio bacteriovorus
- PutA complex
- 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
- 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
- 2rbf – EcPutA DNA-binding domain + DNA
- 4o8a – EcPutA DNA-binding + PRODH domains + FAD
- 4h6q – DrPutA + FAD + THF
- 3haz - PutA + FAD + NAD - Bradyrhyzobium japonicum
- 5ux5 - PutA + FAD + NAD - Corynebacterium freiburgense
- 5kf6, 5kf7 - PutA + FAD + NAD + THF - Sinorhizobium meliloti
- 2jxi - PpPutA DNA-binding domain + DNA
References
