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New page: left|200px<br /><applet load="1npx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1npx, resolution 2.16Å" /> '''STRUCTURE OF NADH PE...
 
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[[Image:1npx.jpg|left|200px]]<br /><applet load="1npx" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1npx.jpg|left|200px]]<br /><applet load="1npx" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1npx, resolution 2.16&Aring;" />
caption="1npx, resolution 2.16&Aring;" />
'''STRUCTURE OF NADH PEROXIDASE FROM STREPTOCOCCUS FAECALIS 10C1 REFINED AT 2.16 ANGSTROMS RESOLUTION'''<br />
'''STRUCTURE OF NADH PEROXIDASE FROM STREPTOCOCCUS FAECALIS 10C1 REFINED AT 2.16 ANGSTROMS RESOLUTION'''<br />


==Overview==
==Overview==
The crystal structure of NADH peroxidase (EC 1.11.1.1) from Streptococcus, faecalis 10C1 (Enterococcus faecalis) has been refined to a resolution of, 2.16 A using the simulated annealing method. The final crystallographic, R-factor is 17.7% for all data in the resolution range 7 to 2.16 A. The, standard deviations are 0.015 A in bond lengths and 3.0 degrees in bond, angles for the final model, which includes all 447 amino acid residues, one FAD and 369 water molecules. The enzyme is a symmetrical tetramer with, point group D2; the symmetry is crystallographic. The redox center of the, enzyme consists of FAD and a cysteine (Cys42), which forms a sulfenic acid, (Cys-SOH) in its oxidized state. A histidine (His10) close to Cys42 is, likely to act as an active-site base. In the analyzed crystal, the enzyme, was in a non-native oxidation state with Cys42 oxidized to a sulfonic acid, Cys-SO3H. The chain fold of NADH peroxidase is similar to those of, disulfide oxidoreductases. A comparison with glutathione reductase, a, representative of this enzyme family, is given.
The crystal structure of NADH peroxidase (EC 1.11.1.1) from Streptococcus faecalis 10C1 (Enterococcus faecalis) has been refined to a resolution of 2.16 A using the simulated annealing method. The final crystallographic R-factor is 17.7% for all data in the resolution range 7 to 2.16 A. The standard deviations are 0.015 A in bond lengths and 3.0 degrees in bond angles for the final model, which includes all 447 amino acid residues, one FAD and 369 water molecules. The enzyme is a symmetrical tetramer with point group D2; the symmetry is crystallographic. The redox center of the enzyme consists of FAD and a cysteine (Cys42), which forms a sulfenic acid (Cys-SOH) in its oxidized state. A histidine (His10) close to Cys42 is likely to act as an active-site base. In the analyzed crystal, the enzyme was in a non-native oxidation state with Cys42 oxidized to a sulfonic acid Cys-SO3H. The chain fold of NADH peroxidase is similar to those of disulfide oxidoreductases. A comparison with glutathione reductase, a representative of this enzyme family, is given.


==About this Structure==
==About this Structure==
1NPX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis] with CYO and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/NADH_peroxidase NADH peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.1 1.11.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NPX OCA].  
1NPX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis] with <scene name='pdbligand=CYO:'>CYO</scene> and <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/NADH_peroxidase NADH peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.1 1.11.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NPX OCA].  


==Reference==
==Reference==
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[[Category: NADH peroxidase]]
[[Category: NADH peroxidase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Ahmed, S.A.]]
[[Category: Ahmed, S A.]]
[[Category: Claiborne, A.]]
[[Category: Claiborne, A.]]
[[Category: Schulz, G.E.]]
[[Category: Schulz, G E.]]
[[Category: Stehle, T.]]
[[Category: Stehle, T.]]
[[Category: CYO]]
[[Category: CYO]]
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[[Category: oxidoreductase(h2o2(a))]]
[[Category: oxidoreductase(h2o2(a))]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:08:49 2008''