1jb9
From Proteopedia
(New page: 200px<br /><applet load="1jb9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jb9, resolution 1.7Å" /> '''Crystal Structure of ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1jb9.gif|left|200px]]<br /><applet load="1jb9" size=" | + | [[Image:1jb9.gif|left|200px]]<br /><applet load="1jb9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jb9, resolution 1.7Å" /> | caption="1jb9, resolution 1.7Å" /> | ||
'''Crystal Structure of The Ferredoxin:NADP+ Reductase From Maize Root AT 1.7 Angstroms'''<br /> | '''Crystal Structure of The Ferredoxin:NADP+ Reductase From Maize Root AT 1.7 Angstroms'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Distinct forms of ferredoxin-NADP(+) reductase are expressed in | + | Distinct forms of ferredoxin-NADP(+) reductase are expressed in photosynthetic and nonphotosynthetic plant tissues. Both enzymes catalyze electron transfer between NADP(H) and ferredoxin; whereas in leaves the enzyme transfers reducing equivalents from photoreduced ferredoxin to NADP(+) in photosynthesis, in roots it has the opposite physiological role, reducing ferredoxin at the expense of NADPH mainly for use in nitrate assimilation. Here, structural and kinetic properties of a nonphotosynthetic isoform were analyzed to define characteristics that may be related to tissue-specific function. Compared with spinach leaf ferredoxin-NADP(+) reductase, the recombinant corn root isoform showed a slightly altered absorption spectrum, a higher pI, a >30-fold higher affinity for NADP(+), greater susceptibility to limited proteolysis, and an approximately 20 mV more positive redox potential. The 1.7 A resolution crystal structure is very similar to the structures of ferredoxin-NADP(+) reductases from photosynthetic tissues. Four distinct structural features of this root ferredoxin-NADP(+) reductases are an alternate conformation of the bound FAD molecule, an alternate path for the amino-terminal extension, a disulfide bond in the FAD-binding domain, and changes in the surface that binds ferredoxin. |
==About this Structure== | ==About this Structure== | ||
| - | 1JB9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] with FAD as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1JB9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] with <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1JB9 OCA]. |
==Reference== | ==Reference== | ||
| Line 15: | Line 15: | ||
[[Category: Zea mays]] | [[Category: Zea mays]] | ||
[[Category: Aliverti, A.]] | [[Category: Aliverti, A.]] | ||
| - | [[Category: Faber, H | + | [[Category: Faber, H R.]] |
[[Category: Ferioli, C.]] | [[Category: Ferioli, C.]] | ||
| - | [[Category: Karplus, P | + | [[Category: Karplus, P A.]] |
[[Category: Spinola, M.]] | [[Category: Spinola, M.]] | ||
[[Category: FAD]] | [[Category: FAD]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:20:39 2008'' |
Revision as of 11:20, 21 February 2008
|
Crystal Structure of The Ferredoxin:NADP+ Reductase From Maize Root AT 1.7 Angstroms
Overview
Distinct forms of ferredoxin-NADP(+) reductase are expressed in photosynthetic and nonphotosynthetic plant tissues. Both enzymes catalyze electron transfer between NADP(H) and ferredoxin; whereas in leaves the enzyme transfers reducing equivalents from photoreduced ferredoxin to NADP(+) in photosynthesis, in roots it has the opposite physiological role, reducing ferredoxin at the expense of NADPH mainly for use in nitrate assimilation. Here, structural and kinetic properties of a nonphotosynthetic isoform were analyzed to define characteristics that may be related to tissue-specific function. Compared with spinach leaf ferredoxin-NADP(+) reductase, the recombinant corn root isoform showed a slightly altered absorption spectrum, a higher pI, a >30-fold higher affinity for NADP(+), greater susceptibility to limited proteolysis, and an approximately 20 mV more positive redox potential. The 1.7 A resolution crystal structure is very similar to the structures of ferredoxin-NADP(+) reductases from photosynthetic tissues. Four distinct structural features of this root ferredoxin-NADP(+) reductases are an alternate conformation of the bound FAD molecule, an alternate path for the amino-terminal extension, a disulfide bond in the FAD-binding domain, and changes in the surface that binds ferredoxin.
About this Structure
1JB9 is a Single protein structure of sequence from Zea mays with as ligand. Active as Ferredoxin--NADP(+) reductase, with EC number 1.18.1.2 Full crystallographic information is available from OCA.
Reference
Biochemical and crystallographic characterization of ferredoxin-NADP(+) reductase from nonphotosynthetic tissues., Aliverti A, Faber R, Finnerty CM, Ferioli C, Pandini V, Negri A, Karplus PA, Zanetti G, Biochemistry. 2001 Dec 4;40(48):14501-8. PMID:11724563
Page seeded by OCA on Thu Feb 21 13:20:39 2008
