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1joa

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[[Image:1joa.jpg|left|200px]]<br /><applet load="1joa" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1joa.jpg|left|200px]]<br /><applet load="1joa" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1joa, resolution 2.8&Aring;" />
caption="1joa, resolution 2.8&Aring;" />
'''NADH PEROXIDASE WITH CYSTEINE-SULFENIC ACID'''<br />
'''NADH PEROXIDASE WITH CYSTEINE-SULFENIC ACID'''<br />
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==About this Structure==
==About this Structure==
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1JOA 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 FAD as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Known structural/functional Site: <scene name='pdbsite=ACT:Cso 42 Is The Native, Active CYS-Sulfenic Acid (Soh)'>ACT</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JOA OCA].
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1JOA 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=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Known structural/functional Site: <scene name='pdbsite=ACT:Cso+42+Is+The+Native,+Active+CYS-Sulfenic+Acid+(Soh)'>ACT</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JOA OCA].
==Reference==
==Reference==
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 16:38:26 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:51:03 2008''

Revision as of 07:51, 3 February 2008


1joa, resolution 2.8Å

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NADH PEROXIDASE WITH CYSTEINE-SULFENIC ACID

Overview

In order to obtain the crystal structure of the flavoprotein NADH, peroxidase with its native Cys42-sulfenic acid redox center, a strategy, combining reduced exposure of crystals to ambient oxygen and data, collection at -160 degrees C was applied. The structure of the native, enzyme to 2.8 A resolution is described; these results conclusively, establish the existence of the Cys42-sulfenic acid as the functional, non-flavin redox center of the peroxidase and provide the first structure, for any naturally occurring protein-sulfenic acid. The Cys42-sulfenic acid, atoms C alpha-C beta-S gamma-O roughly define a planar arrangement which, is stacked parallel to the si face of the FAD isoalloxazine and positions, the sulfenyl oxygen atom only 3.3 A from FAD-C4A. His10-N epsilon 2, contributes a hydrogen bond to the sulfenic acid oxygen, at a distance of, 3.2 A. Although one oxygen atom (OX1) of the non-native Cys42-sulfonic, acid derivative identified in the earlier wild-type peroxidase structure, was taken to represent the native Cys42-sulfenic acid oxygen [Stehle, T., Ahmed, S. A., Claiborne, A., & Schulz, G. E. (1991) J. Mol. Biol. 221, 1325-1344], this structure shows that the sulfenic acid oxygen does not, occupy this position, nor is it hydrogen-bonded to Cys42-N as was OX1., Comparison of the native Cys42-sulfenic acid structure with that of, two-electron reduced glutathione reductase provides an insight into the, sulfenic acid FAD charge-transfer interaction observed with both wild-type, and His10 mutant peroxidases. A model of the E.NADH intermediate recently, observed in stopped-flow analyses of the enzyme [Crane, E. J., III, Parsonage, D., Poole, L. B., & Claiborne, A. (1995) Biochemistry 34, 14114-14124] has also been generated to assist in analyzing the chemical, mechanism of sulfenic acid reduction.

About this Structure

1JOA is a Single protein structure of sequence from Enterococcus faecalis with as ligand. Active as NADH peroxidase, with EC number 1.11.1.1 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Structure of the native cysteine-sulfenic acid redox center of enterococcal NADH peroxidase refined at 2.8 A resolution., Yeh JI, Claiborne A, Hol WG, Biochemistry. 1996 Aug 6;35(31):9951-7. PMID:8756456

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