2ghh: Difference between revisions
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[[Image:2ghh.gif|left|200px]] | [[Image:2ghh.gif|left|200px]] | ||
'''Conformational mobility in the active site of a heme peroxidase''' | {{Structure | ||
|PDB= 2ghh |SIZE=350|CAPTION= <scene name='initialview01'>2ghh</scene>, resolution 2.013Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=NO:NITROGEN OXIDE'>NO</scene> | |||
|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] | |||
|GENE= ascorbate peroxidase ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3847 Glycine max]) | |||
}} | |||
'''Conformational mobility in the active site of a heme peroxidase''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2GHH is a [ | 2GHH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GHH OCA]. | ||
==Reference== | ==Reference== | ||
Conformational mobility in the active site of a heme peroxidase., Badyal SK, Joyce MG, Sharp KH, Seward HE, Mewies M, Basran J, Macdonald IK, Moody PC, Raven EL, J Biol Chem. 2006 Aug 25;281(34):24512-20. Epub 2006 Jun 7. PMID:[http:// | Conformational mobility in the active site of a heme peroxidase., Badyal SK, Joyce MG, Sharp KH, Seward HE, Mewies M, Basran J, Macdonald IK, Moody PC, Raven EL, J Biol Chem. 2006 Aug 25;281(34):24512-20. Epub 2006 Jun 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16762924 16762924] | ||
[[Category: Glycine max]] | [[Category: Glycine max]] | ||
[[Category: L-ascorbate peroxidase]] | [[Category: L-ascorbate peroxidase]] | ||
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[[Category: orthogonal bundle]] | [[Category: orthogonal bundle]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:04:44 2008'' | ||
Revision as of 18:04, 20 March 2008
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| , resolution 2.013Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Gene: | ascorbate peroxidase (Glycine max) | ||||||
| Activity: | L-ascorbate peroxidase, with EC number 1.11.1.11 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Conformational mobility in the active site of a heme peroxidase
OverviewOverview
Conformational mobility of the distal histidine residue has been implicated for several different heme peroxidase enzymes, but unambiguous structural evidence is not available. In this work, we present mechanistic, spectroscopic, and structural evidence for peroxide- and ligand-induced conformational mobility of the distal histidine residue (His-42) in a site-directed variant of ascorbate peroxidase (W41A). In this variant, His-42 binds "on" to the heme in the oxidized form, duplicating the active site structure of the cytochromes b but, in contrast to the cytochromes b, is able to swing "off" the iron during catalysis. This conformational flexibility between the on and off forms is fully reversible and is used as a means to overcome the inherently unreactive nature of the on form toward peroxide, so that essentially complete catalytic activity is maintained. Contrary to the widely adopted view of heme enzyme catalysis, these data indicate that strong coordination of the distal histidine to the heme iron does not automatically undermine catalytic activity. The data add a new dimension to our wider appreciation of structure/activity correlations in other heme enzymes.
About this StructureAbout this Structure
2GHH is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.
ReferenceReference
Conformational mobility in the active site of a heme peroxidase., Badyal SK, Joyce MG, Sharp KH, Seward HE, Mewies M, Basran J, Macdonald IK, Moody PC, Raven EL, J Biol Chem. 2006 Aug 25;281(34):24512-20. Epub 2006 Jun 7. PMID:16762924
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