1apx

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|PDB= 1apx |SIZE=350|CAPTION= <scene name='initialview01'>1apx</scene>, resolution 2.2&Aring;
|PDB= 1apx |SIZE=350|CAPTION= <scene name='initialview01'>1apx</scene>, resolution 2.2&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> and <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene>
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/L-ascorbate_peroxidase L-ascorbate peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.11 1.11.1.11]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/L-ascorbate_peroxidase L-ascorbate peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.11 1.11.1.11] </span>
|GENE= CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3888 Pisum sativum])
|GENE= CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3888 Pisum sativum])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1apx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apx OCA], [http://www.ebi.ac.uk/pdbsum/1apx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1apx RCSB]</span>
}}
}}
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[[Category: Patterson, W R.]]
[[Category: Patterson, W R.]]
[[Category: Poulos, T L.]]
[[Category: Poulos, T L.]]
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[[Category: HEM]]
 
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[[Category: K]]
 
[[Category: peroxidase]]
[[Category: peroxidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:00:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:45:10 2008''

Revision as of 15:45, 30 March 2008


PDB ID 1apx

Drag the structure with the mouse to rotate
, resolution 2.2Å
Ligands: ,
Gene: CDNA (Pisum sativum)
Activity: L-ascorbate peroxidase, with EC number 1.11.1.11
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF RECOMBINANT ASCORBATE PEROXIDASE


Overview

The crystal structure of recombinant pea cytosolic ascorbate peroxidase has been refined to an R = 0.19 for data between 8.0 and 2.2 A resolution and magnitude of F > or = 2 sigma(magnitude of F). The refined model consists of four ascorbate peroxidase monomers consisting of 249 residues per monomer assembled into two homodimers, with one heme group per monomer. The ascorbate peroxidase model confirms that the pea cytosolic enzyme is a noncovalent homodimer held together by a series of ionic interactions arranged around the 2-fold noncrystallographic dimer axis. As expected from the high level of sequence identity (33%), the overall fold of the ascorbate peroxidase monomer closely resembles that of cytochrome c peroxidase. The average root mean square differences for 137 helical alpha-carbon atoms between the four ascorbate peroxidase monomers and cytochrome c peroxidase and for 249 topologically equivalent alpha-carbon atoms are 0.9 and 1.3 A, respectively. The active site structures are also the same, including the hydrogen-bonding interactions between the proximal His ligand, a buried Asp residue, and a Trp residue, whose indole ring is parallel to and in contact with the proximal His ligand just under the heme ring. This proximal Trp residue is thought to be the site of free radical formation in cytochrome c peroxidase compound I and is also essential for enzyme activity. The corresponding Trp in ascorbate peroxidase, Trp179, occupies exactly the same position. The most interesting, and possibly functionally important, difference between the two peroxidases is the presence of a cation binding site in ascorbate peroxidase located approximately 8 A from the alpha-carbon atom of Trp179.

About this Structure

1APX is a Single protein structure of sequence from Pisum sativum. Full crystallographic information is available from OCA.

Reference

Crystal structure of recombinant pea cytosolic ascorbate peroxidase., Patterson WR, Poulos TL, Biochemistry. 1995 Apr 4;34(13):4331-41. PMID:7703247

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