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2e3a

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{{STRUCTURE_2e3a| PDB=2e3a | SCENE= }}
{{STRUCTURE_2e3a| PDB=2e3a | SCENE= }}
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'''Crystal structure of the NO-bound form of Arthromyces ramosus peroxidase at 1.3 Angstroms resolution'''
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===Crystal structure of the NO-bound form of Arthromyces ramosus peroxidase at 1.3 Angstroms resolution===
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==Overview==
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1.3 A resolution crystal structures of the cyanide, nitric oxide and hydroxylamine complexes of Arthromyces ramosus peroxidase (ARP), a class II peroxidase belonging to the plant peroxidase superfamily, have been determined. Anisotropic temperature factors were introduced for all non-H atoms of these complexes using SHELX-97 and stereochemical constraints were applied to the protein, protoporphyrin and sugar moieties, but not to the coordination geometries to the haem iron. These refinements identified multiple conformations for several side chains and revised the side-chain conformations of several residues. Little difference was observed in the structures of the polypeptides, haem and sugar moieties and in the coordinations to two calcium ions in these complexes. Characteristic coordination geometries of each ligand to the haem iron were observed. CN(-) binds to the haem iron in a tilt mode (Fe...C-N = 170 degrees ), whereas NO and hydroxylamine bind in bent modes (Fe...N-O = 125 degrees and Fe...NH(2)-OH = 111 degrees ). CN(-) is directed toward the distal histidine (His56) and forms a hydrogen bond with the N(epsilon) atom, whereas NO and hydroxylamine are directed away from His56. The Fe atoms of ARP-CN and ARP-NO, in which the haem irons are both in low-spin states, are approximately in the pyrrole N plane, whereas the iron in native ARP, which is in a five-coordinated high-spin state, deviates markedly from the plane.
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{{ABSTRACT_PUBMED_17372351}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Structures of cyanide, nitric oxide and hydroxylamine complexes of Arthromyces ramosusperoxidase at 100 K refined to 1.3 A resolution: coordination geometries of the ligands to the haem iron., Fukuyama K, Okada T, Acta Crystallogr D Biol Crystallogr. 2007 Apr;63(Pt 4):472-7. Epub 2007, Mar 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17372351 17372351]
Structures of cyanide, nitric oxide and hydroxylamine complexes of Arthromyces ramosusperoxidase at 100 K refined to 1.3 A resolution: coordination geometries of the ligands to the haem iron., Fukuyama K, Okada T, Acta Crystallogr D Biol Crystallogr. 2007 Apr;63(Pt 4):472-7. Epub 2007, Mar 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17372351 17372351]
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Crystal structure of the fungal peroxidase from Arthromyces ramosus at 1.9 A resolution. Structural comparisons with the lignin and cytochrome c peroxidases., Kunishima N, Fukuyama K, Matsubara H, Hatanaka H, Shibano Y, Amachi T, J Mol Biol. 1994 Jan 7;235(1):331-44. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8289254 8289254]
[[Category: Eukaryota]]
[[Category: Eukaryota]]
[[Category: Peroxidase]]
[[Category: Peroxidase]]
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[[Category: Heme protein]]
[[Category: Heme protein]]
[[Category: Peroxidase]]
[[Category: Peroxidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:50:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:06:01 2008''

Revision as of 11:06, 29 July 2008

Image:2e3a.png

Template:STRUCTURE 2e3a

Crystal structure of the NO-bound form of Arthromyces ramosus peroxidase at 1.3 Angstroms resolution

Template:ABSTRACT PUBMED 17372351

About this Structure

2E3A is a Single protein structure of sequence from Eukaryota. Full crystallographic information is available from OCA.

Reference

Structures of cyanide, nitric oxide and hydroxylamine complexes of Arthromyces ramosusperoxidase at 100 K refined to 1.3 A resolution: coordination geometries of the ligands to the haem iron., Fukuyama K, Okada T, Acta Crystallogr D Biol Crystallogr. 2007 Apr;63(Pt 4):472-7. Epub 2007, Mar 16. PMID:17372351

Crystal structure of the fungal peroxidase from Arthromyces ramosus at 1.9 A resolution. Structural comparisons with the lignin and cytochrome c peroxidases., Kunishima N, Fukuyama K, Matsubara H, Hatanaka H, Shibano Y, Amachi T, J Mol Biol. 1994 Jan 7;235(1):331-44. PMID:8289254

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