1bqe
From Proteopedia
(New page: 200px<br /><applet load="1bqe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bqe, resolution 2.45Å" /> '''FERREDOXIN:NADP+ RED...) |
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| - | [[Image:1bqe.jpg|left|200px]]<br /><applet load="1bqe" size=" | + | [[Image:1bqe.jpg|left|200px]]<br /><applet load="1bqe" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bqe, resolution 2.45Å" /> | caption="1bqe, resolution 2.45Å" /> | ||
'''FERREDOXIN:NADP+ REDUCTASE MUTANT WITH THR 155 REPLACED BY GLY (T155G)'''<br /> | '''FERREDOXIN:NADP+ REDUCTASE MUTANT WITH THR 155 REPLACED BY GLY (T155G)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | On the basis of sequence and three-dimensional structure comparison | + | On the basis of sequence and three-dimensional structure comparison between Anabaena PCC7119 ferredoxin-NADP(+) reductase (FNR) and other reductases from its structurally related family that bind either NADP(+)/H or NAD(+)/H, a set of amino acid residues that might determine the FNR coenzyme specificity can be assigned. These residues include Thr-155, Ser-223, Arg-224, Arg-233 and Tyr-235. Systematic replacement of these amino acids was done to identify which of them are the main determinants of coenzyme specificity. Our data indicate that all of the residues interacting with the 2'-phosphate of NADP(+)/H in Anabaena FNR are not involved to the same extent in determining coenzyme specificity and affinity. Thus, it is found that Ser-223 and Tyr-235 are important for determining NADP(+)/H specificity and orientation with respect to the protein, whereas Arg-224 and Arg-233 provide only secondary interactions in Anabaena FNR. The analysis of the T155G FNR form also indicates that the determinants of coenzyme specificity are not only situated in the 2'-phosphate NADP(+)/H interacting region but that other regions of the protein must be involved. These regions, although not interacting directly with the coenzyme, must produce specific structural arrangements of the backbone chain that determine coenzyme specificity. The loop formed by residues 261-268 in Anabaena FNR must be one of these regions. |
==About this Structure== | ==About this Structure== | ||
| - | 1BQE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.] with SO4 and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ferredoxin--NADP(+)_reductase Ferredoxin--NADP(+) reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.1.2 1.18.1.2] Full crystallographic information is available from [http:// | + | 1BQE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ferredoxin--NADP(+)_reductase Ferredoxin--NADP(+) reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.1.2 1.18.1.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BQE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Gomez-Moreno, C.]] | [[Category: Gomez-Moreno, C.]] | ||
| - | [[Category: Hermoso, J | + | [[Category: Hermoso, J A.]] |
[[Category: Martinez-Julvez, M.]] | [[Category: Martinez-Julvez, M.]] | ||
[[Category: Martinez-Ripoll, M.]] | [[Category: Martinez-Ripoll, M.]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:57:57 2008'' |
Revision as of 09:57, 21 February 2008
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FERREDOXIN:NADP+ REDUCTASE MUTANT WITH THR 155 REPLACED BY GLY (T155G)
Overview
On the basis of sequence and three-dimensional structure comparison between Anabaena PCC7119 ferredoxin-NADP(+) reductase (FNR) and other reductases from its structurally related family that bind either NADP(+)/H or NAD(+)/H, a set of amino acid residues that might determine the FNR coenzyme specificity can be assigned. These residues include Thr-155, Ser-223, Arg-224, Arg-233 and Tyr-235. Systematic replacement of these amino acids was done to identify which of them are the main determinants of coenzyme specificity. Our data indicate that all of the residues interacting with the 2'-phosphate of NADP(+)/H in Anabaena FNR are not involved to the same extent in determining coenzyme specificity and affinity. Thus, it is found that Ser-223 and Tyr-235 are important for determining NADP(+)/H specificity and orientation with respect to the protein, whereas Arg-224 and Arg-233 provide only secondary interactions in Anabaena FNR. The analysis of the T155G FNR form also indicates that the determinants of coenzyme specificity are not only situated in the 2'-phosphate NADP(+)/H interacting region but that other regions of the protein must be involved. These regions, although not interacting directly with the coenzyme, must produce specific structural arrangements of the backbone chain that determine coenzyme specificity. The loop formed by residues 261-268 in Anabaena FNR must be one of these regions.
About this Structure
1BQE is a Single protein structure of sequence from Anabaena sp. with and as ligands. Active as Ferredoxin--NADP(+) reductase, with EC number 1.18.1.2 Full crystallographic information is available from OCA.
Reference
Probing the determinants of coenzyme specificity in ferredoxin-NADP+ reductase by site-directed mutagenesis., Medina M, Luquita A, Tejero J, Hermoso J, Mayoral T, Sanz-Aparicio J, Grever K, Gomez-Moreno C, J Biol Chem. 2001 Apr 13;276(15):11902-12. Epub 2001 Jan 4. PMID:11152461
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