1ew6
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1ew6 |SIZE=350|CAPTION= <scene name='initialview01'>1ew6</scene>, resolution 1.78Å | |PDB= 1ew6 |SIZE=350|CAPTION= <scene name='initialview01'>1ew6</scene>, resolution 1.78Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ewa|1EWA]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ew6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ew6 OCA], [http://www.ebi.ac.uk/pdbsum/1ew6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ew6 RCSB]</span> | ||
}} | }} | ||
| Line 23: | Line 26: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Lebioda, L.]] | [[Category: Lebioda, L.]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: SO4]] | ||
[[Category: globin]] | [[Category: globin]] | ||
[[Category: halophenol]] | [[Category: halophenol]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:10:58 2008'' |
Revision as of 17:11, 30 March 2008
| |||||||
| , resolution 1.78Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1EWA
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Sun Mar 30 20:10:58 2008
