Proline utilization A
From Proteopedia
(Difference between revisions)
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**[[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 | ||
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**[[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 | + | **[[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 /> | ||
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**[[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
|
3D Structures of proline utilization A
Updated on 19-September-2017
References
- ↑ 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