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1npx

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{{STRUCTURE_1npx| PDB=1npx | SCENE= }}
{{STRUCTURE_1npx| PDB=1npx | SCENE= }}
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'''STRUCTURE OF NADH PEROXIDASE FROM STREPTOCOCCUS FAECALIS 10C1 REFINED AT 2.16 ANGSTROMS RESOLUTION'''
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===STRUCTURE OF NADH PEROXIDASE FROM STREPTOCOCCUS FAECALIS 10C1 REFINED AT 2.16 ANGSTROMS RESOLUTION===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_1942054}}
==About this Structure==
==About this Structure==
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[[Category: Schulz, G E.]]
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[[Category: Stehle, T.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:10:19 2008''

Revision as of 23:10, 28 July 2008

Image:1npx.png

Template:STRUCTURE 1npx

STRUCTURE OF NADH PEROXIDASE FROM STREPTOCOCCUS FAECALIS 10C1 REFINED AT 2.16 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 1942054

About this Structure

1NPX is a Single protein structure of sequence from Enterococcus faecalis. Full crystallographic information is available from OCA.

Reference

Structure of NADH peroxidase from Streptococcus faecalis 10C1 refined at 2.16 A resolution., Stehle T, Ahmed SA, Claiborne A, Schulz GE, J Mol Biol. 1991 Oct 20;221(4):1325-44. PMID:1942054

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