2gas: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /><applet load="2gas" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gas, resolution 1.6Å" /> '''Crystal Structure of ...
 
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:2gas.gif|left|200px]]<br /><applet load="2gas" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2gas.gif|left|200px]]<br /><applet load="2gas" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2gas, resolution 1.6&Aring;" />
caption="2gas, resolution 1.6&Aring;" />
'''Crystal Structure of Isoflavone Reductase'''<br />
'''Crystal Structure of Isoflavone Reductase'''<br />


==Overview==
==Overview==
Isoflavonoids play important roles in plant defense and exhibit a range of, mammalian health-promoting activities. Isoflavone reductase (IFR), specifically recognizes isoflavones and catalyzes a stereospecific, NADPH-dependent reduction to (3R)-isoflavanone. The crystal structure of, Medicago sativa IFR with deletion of residues 39-47 has been determined at, 1.6A resolution. Structural analysis, molecular modeling and docking, and, comparison with the structures of other NADPH-dependent enzymes, defined, the putative binding sites for co-factor and substrate and potential key, residues for enzyme activity and substrate specificity. Further, mutagenesis has confirmed the role of Lys144 as a catalytic residue. This, study provides a structural basis for understanding the enzymatic, mechanism and substrate specificity of IFRs as well as the functions of, IFR-like proteins.
Isoflavonoids play important roles in plant defense and exhibit a range of mammalian health-promoting activities. Isoflavone reductase (IFR) specifically recognizes isoflavones and catalyzes a stereospecific NADPH-dependent reduction to (3R)-isoflavanone. The crystal structure of Medicago sativa IFR with deletion of residues 39-47 has been determined at 1.6A resolution. Structural analysis, molecular modeling and docking, and comparison with the structures of other NADPH-dependent enzymes, defined the putative binding sites for co-factor and substrate and potential key residues for enzyme activity and substrate specificity. Further mutagenesis has confirmed the role of Lys144 as a catalytic residue. This study provides a structural basis for understanding the enzymatic mechanism and substrate specificity of IFRs as well as the functions of IFR-like proteins.


==About this Structure==
==About this Structure==
2GAS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Medicago_sativa Medicago sativa]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2GAS OCA].  
2GAS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Medicago_sativa Medicago sativa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GAS OCA].  


==Reference==
==Reference==
Line 14: Line 14:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Chang, Z.]]
[[Category: Chang, Z.]]
[[Category: Dixon, R.A.]]
[[Category: Dixon, R A.]]
[[Category: He, X.]]
[[Category: He, X.]]
[[Category: Lin, J.]]
[[Category: Lin, J.]]
Line 21: Line 21:
[[Category: nadph-dependent reductase]]
[[Category: nadph-dependent reductase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:05:04 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:29:51 2008''