1bgp

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[[Image:1bgp.gif|left|200px]]<br /><applet load="1bgp" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1bgp.gif|left|200px]]
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caption="1bgp, resolution 1.90&Aring;" />
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'''CRYSTAL STRUCTURE OF BARLEY GRAIN PEROXIDASE 1'''<br />
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{{Structure
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|PDB= 1bgp |SIZE=350|CAPTION= <scene name='initialview01'>1bgp</scene>, resolution 1.90&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> and <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Peroxidase Peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF BARLEY GRAIN PEROXIDASE 1'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1BGP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Peroxidase Peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BGP OCA].
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1BGP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BGP OCA].
==Reference==
==Reference==
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Structure of barley grain peroxidase refined at 1.9-A resolution. A plant peroxidase reversibly inactivated at neutral pH., Henriksen A, Welinder KG, Gajhede M, J Biol Chem. 1998 Jan 23;273(4):2241-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9442067 9442067]
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Structure of barley grain peroxidase refined at 1.9-A resolution. A plant peroxidase reversibly inactivated at neutral pH., Henriksen A, Welinder KG, Gajhede M, J Biol Chem. 1998 Jan 23;273(4):2241-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9442067 9442067]
[[Category: Hordeum vulgare]]
[[Category: Hordeum vulgare]]
[[Category: Peroxidase]]
[[Category: Peroxidase]]
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[[Category: peroxidase]]
[[Category: peroxidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:55:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:10:46 2008''

Revision as of 08:10, 20 March 2008

Image:1bgp.gif


PDB ID 1bgp

Drag the structure with the mouse to rotate
, resolution 1.90Å
Ligands: , and
Activity: Peroxidase, with EC number 1.11.1.7
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF BARLEY GRAIN PEROXIDASE 1


Overview

The crystal structure of the major peroxidase of barley grain (BP 1) has been solved by molecular replacement and phase combination and refined to an R-factor of 19.2% for all data between 38 and 1.9 A. The refined model includes amino acid residues 1-309, one calcium ion, one sodium ion, iron-protoporphyrin IX, and 146 solvent molecules. BP 1 has the apparently unique property of being unable to catalyze the reaction with the primary substrate hydrogen peroxide to form compound I at pH values > 5, a feature investigated by obtaining crystal structure data at pH 5.5, 7.5, and 8.5. Structural comparison shows that the overall fold of inactive barley grain peroxidase at these pH values resembles that of both horseradish peroxidase C and peanut peroxidase. The key differences between the structures of active horseradish peroxidase C and inactive BP 1 include the orientation of the catalytic distal histidine, disruption of a hydrogen bond between this histidine and a conserved asparagine, and apparent substitution of calcium at the distal cation binding site with sodium at pH 7.5. These profound changes are a result of a dramatic structural rearrangement to the loop region between helices B and C. This is the first time that structural rearrangements linked to active site chemistry have been observed by crystallography in the peroxidase domain distal to heme.

About this Structure

1BGP is a Single protein structure of sequence from Hordeum vulgare. Full crystallographic information is available from OCA.

Reference

Structure of barley grain peroxidase refined at 1.9-A resolution. A plant peroxidase reversibly inactivated at neutral pH., Henriksen A, Welinder KG, Gajhede M, J Biol Chem. 1998 Jan 23;273(4):2241-8. PMID:9442067

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