'''STRUCTURE OF FERREDOXIN-NADP+ REDUCTASE WITH GLU 139 REPLACED BY LYS (E139K)'''
===STRUCTURE OF FERREDOXIN-NADP+ REDUCTASE WITH GLU 139 REPLACED BY LYS (E139K)===
==Overview==
<!--
The role of the negative charge of the E139 side-chain of Anabaena Ferredoxin-NADP+ reductase (FNR) in steering appropriate docking with its substrates ferredoxin, flavodoxin and NADP+/H, that leads to efficient electron transfer (ET) is analysed by characterization of several E139 FNR mutants. Replacement of E139 affects the interaction with the different FNR substrates in very different ways. Thus, while E139 does not appear to be involved in the processes of binding and ET between FNR and NADP+/H, the nature and the conformation of the residue at position 139 of Anabaena FNR modulates the precise enzyme interaction with the protein carriers ferredoxin (Fd) and flavodoxin (Fld). Introduction of the shorter aspartic acid side-chain at position 139 produces an enzyme that interacts more weakly with both ET proteins. Moreover, the removal of the charge, as in the E139Q mutant, or the charge-reversal mutation, as in E139K FNR, apparently enhances additional interaction modes of the enzyme with Fd, and reduces the possible orientations with Fld to more productive and stronger ones. Hence, removal of the negative charge at position 139 of Anabaena FNR produces a deleterious effect in its ET reactions with Fd whereas it appears to enhance the ET processes with Fld. Significantly, a large structural variation is observed for the E139 side-chain conformer in different FNR structures, including the E139K mutant. In this case, a positive potential region replaces a negative one in the wild-type enzyme. Our observations further confirm the contribution of both attractive and repulsive interactions in achieving the optimal orientation for efficient ET between FNR and its protein carriers.
The line below this paragraph, {{ABSTRACT_PUBMED_12383252}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 12383252 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_12383252}}
==About this Structure==
==About this Structure==
Line 32:
Line 36:
[[Category: Nadp+ reductase]]
[[Category: Nadp+ reductase]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:54:57 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:56:05 2008''
Revision as of 05:56, 1 July 2008
This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.
STRUCTURE OF FERREDOXIN-NADP+ REDUCTASE WITH GLU 139 REPLACED BY LYS (E139K)STRUCTURE OF FERREDOXIN-NADP+ REDUCTASE WITH GLU 139 REPLACED BY LYS (E139K)
1GR1 is a Single protein structure of sequence from Anabaena sp.. Full crystallographic information is available from OCA.
ReferenceReference
Probing the role of glutamic acid 139 of Anabaena ferredoxin-NADP+ reductase in the interaction with substrates., Faro M, Frago S, Mayoral T, Hermoso JA, Sanz-Aparicio J, Gomez-Moreno C, Medina M, Eur J Biochem. 2002 Oct;269(20):4938-47. PMID:12383252
