1qfz: Difference between revisions

Line 1:

[[Image:1qfz.~~gif~~|left|200px]]

[[Image:1qfz.png|left|200px]]

<!--

Line 9:

Line 10:

~~'''~~PEA FNR Y308S MUTANT IN COMPLEX WITH NADPH~~'''~~

===PEA FNR Y308S MUTANT IN COMPLEX WITH NADPH===

~~==Overview==~~

<!--

The flavoenzyme ferredoxin-NADP+ reductase (FNR) catalyzes the production of NADPH during photosynthesis. Whereas the structures of FNRs from spinach leaf and a cyanobacterium as well as many of their homologs have been solved, ~~none of these studies has yielded a productive geometry of~~ the ~~flavin-nicotinamide interaction. Here, we show that this failure occurs because nicotinamide binding~~ to ~~wild type FNR involves~~ the ~~energetically unfavorable displacement of the C-terminal Tyr side chain. We used mutants of this residue~~ (Tyr 308) of pea FNR to obtain the structures of productive NADP+ and NADPH complexes. These structures reveal a unique NADP+ binding mode in which the nicotinamide ring is not parallel to the flavin isoalloxazine ring, but lies against it at ~~an angle of approximately 30 degrees~~, ~~with the C4 atom 3 A from~~ the ~~flavin N5 atom~~.

The line below this paragraph, {{ABSTRACT_PUBMED_10467097}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10467097 is the PubMed ID number.

-->

==About this Structure==

Line 36:

Line 40:

[[Category: Hydride transfer]]

[[Category: Photosynthesis]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 06~~:13:24 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:49:38 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1qfz.gif|left|200px]]
+{{Seed}}
+[[Image:1qfz.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1qfz|  PDB=1qfz  |  SCENE=  }}
-'''PEA FNR Y308S MUTANT IN COMPLEX WITH NADPH'''
+===PEA FNR Y308S MUTANT IN COMPLEX WITH NADPH===
-==Overview==
+<!--
-The flavoenzyme ferredoxin-NADP+ reductase (FNR) catalyzes the production of NADPH during photosynthesis. Whereas the structures of FNRs from spinach leaf and a cyanobacterium as well as many of their homologs have been solved, none of these studies has yielded a productive geometry of the flavin-nicotinamide interaction. Here, we show that this failure occurs because nicotinamide binding to wild type FNR involves the energetically unfavorable displacement of the C-terminal Tyr side chain. We used mutants of this residue (Tyr 308) of pea FNR to obtain the structures of productive NADP+ and NADPH complexes. These structures reveal a unique NADP+ binding mode in which the nicotinamide ring is not parallel to the flavin isoalloxazine ring, but lies against it at an angle of approximately 30 degrees, with the C4 atom 3 A from the flavin N5 atom.
+The line below this paragraph, {{ABSTRACT_PUBMED_10467097}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10467097 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10467097}}
 ==About this Structure==
@@ Line 36: / Line 40: @@
 [[Category: Hydride transfer]]
 [[Category: Photosynthesis]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:13:24 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:49:38 2008''