We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1sm4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1sm4.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1sm4.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1sm4| PDB=1sm4 | SCENE= }}
{{STRUCTURE_1sm4| PDB=1sm4 | SCENE= }}
-
'''Crystal Structure Analysis of the Ferredoxin-NADP+ Reductase from Paprika'''
+
===Crystal Structure Analysis of the Ferredoxin-NADP+ Reductase from Paprika===
-
==Overview==
+
<!--
-
cDNA of Capsicum annuum Yolo Wonder (paprika) has been prepared from total cellular RNA, and the complete gene encoding paprika ferredoxin-NADP(+) reductase (pFNR) precursor was sequenced and cloned from this cDNA. Fusion to a T7 promoter allowed expression in Escherichia coli. Both native and recombinant pFNR were purified to homogeneity and crystallized. The crystal structure of pFNR has been solved by Patterson search techniques using the structure of spinach ferredoxin-NADP(+) reductase as search model. The structure was refined at 2.5-A resolution to a crystallographic R-factor of 19.8% (R(free) = 26.5%). The overall structure of pFNR is similar to other members of the ferredoxin-NADP(+) reductase family, the major differences concern a long loop (residues 167-177) that forms part of the FAD binding site and some of the variable loops in surface regions. The different orientation of the FAD binding loop leads to a tighter interaction between pFNR and the adenine moiety of FAD. The physiological redox partners [2Fe-2S]-ferredoxin I and NADP(+) were modeled into the native structure of pFNR. The complexes reveal a protein-protein interaction site that is consistent with existing biochemical data and imply possible orientations for the side chain of tyrosine 362, which has to be displaced by the nicotinamide moiety of NADP(+) upon binding. A reasonable electron transfer pathway could be deduced from the modeled structures of the complexes.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11053431}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11053431 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11053431}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Rossmann fold]]
[[Category: Rossmann fold]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:52:23 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:58:18 2008''

Revision as of 20:58, 28 July 2008

Image:1sm4.png

Template:STRUCTURE 1sm4

Crystal Structure Analysis of the Ferredoxin-NADP+ Reductase from Paprika

Template:ABSTRACT PUBMED 11053431

About this Structure

1SM4 is a Single protein structure of sequence from Capsicum annuum. This structure supersedes the now removed PDB entry 1fb3. Full crystallographic information is available from OCA.

Reference

Crystal structure of paprika ferredoxin-NADP+ reductase. Implications for the electron transfer pathway., Dorowski A, Hofmann A, Steegborn C, Boicu M, Huber R, J Biol Chem. 2001 Mar 23;276(12):9253-63. Epub 2000 Oct 26. PMID:11053431

Page seeded by OCA on Mon Jul 28 23:58:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1sm4"
Personal tools