1joa
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(New page: 200px<br /> <applet load="1joa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1joa, resolution 2.8Å" /> '''NADH PEROXIDASE WITH...)
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Revision as of 17:12, 29 October 2007
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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 ... [(full description)]
About this Structure
1JOA is a [Single protein] structure of sequence from [Enterococcus faecalis] with FAD as [ligand]. Active as [[1]], with EC number [1.11.1.1]. 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
Page seeded by OCA on Mon Oct 29 19:17:13 2007
