This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1w87

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1w87.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1w87.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1w87| PDB=1w87 | SCENE= }}
{{STRUCTURE_1w87| PDB=1w87 | SCENE= }}
-
'''FERREDOXIN-NADP REDUCTASE (MUTATION: Y 303 W) COMPLEXED WITH NADP BY COCRYSTALLIZATION'''
+
===FERREDOXIN-NADP REDUCTASE (MUTATION: Y 303 W) COMPLEXED WITH NADP BY COCRYSTALLIZATION===
-
==Overview==
+
<!--
-
Ferredoxin-NADP+ reductase (FNR) catalyzes the reduction of NADP+ to NADPH in an overall reversible reaction, showing some differences in the mechanisms between cyanobacterial and higher plant FNRs. During hydride transfer it is proposed that the FNR C-terminal Tyr is displaced by the nicotinamide. Thus, this C-terminal Tyr might be involved not only in modulating the flavin redox properties, as already shown, but also in nicotinamide binding and hydride transfer. FNR variants from the cyanobacterium Anabaena in which the C-terminal Tyr has been replaced by Trp, Phe, or Ser have been produced. All FNR variants show enhanced NADP+ and NAD+ binding, especially Tyr303Ser, which correlates with a noticeable improvement of NADH-dependent reactions. Nevertheless, the Tyr303Ser variant shows a decrease in the steady-state kcat value with NADPH. Fast kinetic analysis of the hydride transfer shows that the low efficiency observed for this mutant FNR under steady-state conditions is not due to a lack of catalytic ability but rather to the strong enzyme-coenzyme interaction. Three-dimensional structures for Tyr303Ser and Tyr303Trp variants and its complexes with NADP+ show significant differences between plant and cyanobacterial FNRs. Our results suggest that modulation of coenzyme affinity is highly influenced by the strength of the C-terminus-FAD interaction and that subtle changes between plant and cyanobacterial structures are able to modify the energy of that interaction. Additionally, it is shown that the C-terminal Tyr of FNR lowers the affinity for NADP+/H to levels compatible with steady-state turnover during the catalytic cycle, but it is not involved in the hydride transfer itself.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16216071}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16216071 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16216071}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Phycobilisome]]
[[Category: Phycobilisome]]
[[Category: Thylakoid]]
[[Category: Thylakoid]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:17:32 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:36:08 2008''

Revision as of 06:36, 29 July 2008

Image:1w87.png

Template:STRUCTURE 1w87

FERREDOXIN-NADP REDUCTASE (MUTATION: Y 303 W) COMPLEXED WITH NADP BY COCRYSTALLIZATION

Template:ABSTRACT PUBMED 16216071

About this Structure

1W87 is a Single protein structure of sequence from Anabaena sp.. Full crystallographic information is available from OCA.

Reference

C-terminal tyrosine of ferredoxin-NADP+ reductase in hydride transfer processes with NAD(P)+/H., Tejero J, Perez-Dorado I, Maya C, Martinez-Julvez M, Sanz-Aparicio J, Gomez-Moreno C, Hermoso JA, Medina M, Biochemistry. 2005 Oct 18;44(41):13477-90. PMID:16216071

Page seeded by OCA on Tue Jul 29 09:36:08 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1w87"
Personal tools