1ew6

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(New page: 200px<br /><applet load="1ew6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ew6, resolution 1.78&Aring;" /> '''THE CRYSTAL STRUCTUR...)
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'''THE CRYSTAL STRUCTURE AND AMINO ACID SEQUENCE OF DEHALOPEROXIDASE FROM AMPHITRITE ORNATA INDICATE COMMON ANCESTRY WITH GLOBINS'''<br />
'''THE CRYSTAL STRUCTURE AND AMINO ACID SEQUENCE OF DEHALOPEROXIDASE FROM AMPHITRITE ORNATA INDICATE COMMON ANCESTRY WITH GLOBINS'''<br />
==Overview==
==Overview==
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The full-length, protein coding sequence for dehaloperoxidase was obtained, using a reverse genetic approach and a cDNA library from marine worm, Amphitrite ornata. The crystal structure of the dehaloperoxidase (DHP) was, determined by the multiple isomorphous replacement method and was refined, at 1.8-A resolution. The enzyme fold is that of the globin family and, together with the amino acid sequence information, indicates that the, enzyme evolved from an ancient oxygen carrier. The peroxidase activity of, DHP arose mainly through changes in the positions of the proximal and, distal histidines relative to those seen in globins. The structure of a, complex of DHP with 4-iodophenol is also reported, and it shows that in, contrast to larger heme peroxidases DHP binds organic substrates in the, distal cavity. The binding is facilitated by the histidine swinging in and, out of the cavity. The modeled position of the oxygen atom bound to the, heme suggests that the enzymatic reaction proceeds via direct attack of, the oxygen atom on the carbon atom bound to the halogen atom.
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The full-length, protein coding sequence for dehaloperoxidase was obtained using a reverse genetic approach and a cDNA library from marine worm Amphitrite ornata. The crystal structure of the dehaloperoxidase (DHP) was determined by the multiple isomorphous replacement method and was refined at 1.8-A resolution. The enzyme fold is that of the globin family and, together with the amino acid sequence information, indicates that the enzyme evolved from an ancient oxygen carrier. The peroxidase activity of DHP arose mainly through changes in the positions of the proximal and distal histidines relative to those seen in globins. The structure of a complex of DHP with 4-iodophenol is also reported, and it shows that in contrast to larger heme peroxidases DHP binds organic substrates in the distal cavity. The binding is facilitated by the histidine swinging in and out of the cavity. The modeled position of the oxygen atom bound to the heme suggests that the enzymatic reaction proceeds via direct attack of the oxygen atom on the carbon atom bound to the halogen atom.
==About this Structure==
==About this Structure==
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1EW6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Amphitrite_ornata Amphitrite ornata] with SO4 and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EW6 OCA].
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1EW6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Amphitrite_ornata Amphitrite ornata] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EW6 OCA].
==Reference==
==Reference==
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[[Category: halophenols]]
[[Category: halophenols]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:32:07 2008''

Revision as of 10:32, 21 February 2008

Image:1ew6.jpg

1ew6, resolution 1.78Å

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THE CRYSTAL STRUCTURE AND AMINO ACID SEQUENCE OF DEHALOPEROXIDASE FROM AMPHITRITE ORNATA INDICATE COMMON ANCESTRY WITH GLOBINS

Overview

The full-length, protein coding sequence for dehaloperoxidase was obtained using a reverse genetic approach and a cDNA library from marine worm Amphitrite ornata. The crystal structure of the dehaloperoxidase (DHP) was determined by the multiple isomorphous replacement method and was refined at 1.8-A resolution. The enzyme fold is that of the globin family and, together with the amino acid sequence information, indicates that the enzyme evolved from an ancient oxygen carrier. The peroxidase activity of DHP arose mainly through changes in the positions of the proximal and distal histidines relative to those seen in globins. The structure of a complex of DHP with 4-iodophenol is also reported, and it shows that in contrast to larger heme peroxidases DHP binds organic substrates in the distal cavity. The binding is facilitated by the histidine swinging in and out of the cavity. The modeled position of the oxygen atom bound to the heme suggests that the enzymatic reaction proceeds via direct attack of the oxygen atom on the carbon atom bound to the halogen atom.

About this Structure

1EW6 is a Single protein structure of sequence from Amphitrite ornata with and as ligands. Full crystallographic information is available from OCA.

Reference

The crystal structure and amino acid sequence of dehaloperoxidase from Amphitrite ornata indicate common ancestry with globins., LaCount MW, Zhang E, Chen YP, Han K, Whitton MM, Lincoln DE, Woodin SA, Lebioda L, J Biol Chem. 2000 Jun 23;275(25):18712-6. PMID:10751397

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