Proline utilization A

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Line 19: Line 19:
**[[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
Line 27: Line 30:
**[[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 />
Line 38: Line 41:
**[[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/>

Revision as of 18:37, 19 September 2017

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 19-September-2017

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

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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