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| - | [[Image:2atj.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2atj| PDB=2atj | SCENE= }} | | {{STRUCTURE_2atj| PDB=2atj | SCENE= }} |
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| - | '''RECOMBINANT HORSERADISH PEROXIDASE COMPLEX WITH BENZHYDROXAMIC ACID'''
| + | ===RECOMBINANT HORSERADISH PEROXIDASE COMPLEX WITH BENZHYDROXAMIC ACID=== |
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| - | ==Overview==
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| - | The three-dimensional structure of recombinant horseradish peroxidase in complex with BHA (benzhydroxamic acid) is the first structure of a peroxidase-substrate complex demonstrating the existence of an aromatic binding pocket. The crystal structure of the peroxidase-substrate complex has been determined to 2.0 A resolution with a crystallographic R-factor of 0.176 (R-free = 0. 192). A well-defined electron density for BHA is observed in the peroxidase active site, with a hydrophobic pocket surrounding the aromatic ring of the substrate. The hydrophobic pocket is provided by residues H42, F68, G69, A140, P141, and F179 and heme C18, C18-methyl, and C20, with the shortest distance (3.7 A) found between heme C18-methyl and BHA C63. Very little structural rearrangement is seen in the heme crevice in response to substrate binding. F68 moves to form a lid on the hydrophobic pocket, and the distal water molecule moves 0.6 A toward the heme iron. The bound BHA molecule forms an extensive hydrogen bonding network with H42, R38, P139, and the distal water molecule 2.6 A above the heme iron. This remarkably good match in hydrogen bond requirements between the catalytic residues of HRPC and BHA makes the extended interaction between BHA and the distal heme crevice of HRPC possible. Indeed, the ability of BHA to bind to peroxidases, which lack a peripheral hydrophobic pocket, suggests that BHA is a general counterpart for the conserved hydrogen bond donors and acceptors of the distal catalytic site. The closest aromatic residue to BHA is F179, which we predict provides an important hydrophobic interaction with more typical peroxidase substrates.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9609699}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9609699 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9609699}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Oxidoreductase]] | | [[Category: Oxidoreductase]] |
| | [[Category: Peroxidase]] | | [[Category: Peroxidase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:27:33 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:32:29 2008'' |
Revision as of 23:32, 28 July 2008
Template:STRUCTURE 2atj
RECOMBINANT HORSERADISH PEROXIDASE COMPLEX WITH BENZHYDROXAMIC ACID
Template:ABSTRACT PUBMED 9609699
About this Structure
2ATJ is a Single protein structure of sequence from Armoracia rusticana. Full crystallographic information is available from OCA.
Reference
Structural interactions between horseradish peroxidase C and the substrate benzhydroxamic acid determined by X-ray crystallography., Henriksen A, Schuller DJ, Meno K, Welinder KG, Smith AT, Gajhede M, Biochemistry. 1998 Jun 2;37(22):8054-60. PMID:9609699
Page seeded by OCA on Tue Jul 29 02:32:29 2008
