1yi9
From Proteopedia
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| - | [[Image:1yi9.gif|left|200px]] | + | [[Image:1yi9.gif|left|200px]] |
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| - | '''Crystal Structure Analysis of the oxidized form of the M314I mutant of Peptidylglycine alpha-Hydroxylating Monooxygenase''' | + | {{Structure |
| + | |PDB= 1yi9 |SIZE=350|CAPTION= <scene name='initialview01'>1yi9</scene>, resolution 1.70Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Peptidylglycine_monooxygenase Peptidylglycine monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.3 1.14.17.3] | ||
| + | |GENE= Pam ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure Analysis of the oxidized form of the M314I mutant of Peptidylglycine alpha-Hydroxylating Monooxygenase''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YI9 is a [ | + | 1YI9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YI9 OCA]. |
==Reference== | ==Reference== | ||
| - | The catalytic copper of peptidylglycine alpha-hydroxylating monooxygenase also plays a critical structural role., Siebert X, Eipper BA, Mains RE, Prigge ST, Blackburn NJ, Amzel LM, Biophys J. 2005 Nov;89(5):3312-9. Epub 2005 Aug 12. PMID:[http:// | + | The catalytic copper of peptidylglycine alpha-hydroxylating monooxygenase also plays a critical structural role., Siebert X, Eipper BA, Mains RE, Prigge ST, Blackburn NJ, Amzel LM, Biophys J. 2005 Nov;89(5):3312-9. Epub 2005 Aug 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16100265 16100265] |
[[Category: Peptidylglycine monooxygenase]] | [[Category: Peptidylglycine monooxygenase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''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 15:23:10 2008'' |
Revision as of 13:23, 20 March 2008
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| , resolution 1.70Å | |||||||
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| Ligands: | and | ||||||
| Gene: | Pam (Rattus norvegicus) | ||||||
| Activity: | Peptidylglycine monooxygenase, with EC number 1.14.17.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure Analysis of the oxidized form of the M314I mutant of Peptidylglycine alpha-Hydroxylating Monooxygenase
Overview
Many bioactive peptides require amidation of their carboxy terminus to exhibit full biological activity. Peptidylglycine alpha-hydroxylating monooxygenase (PHM; EC 1.14.17.3), the enzyme that catalyzes the first of the two steps of this reaction, is composed of two domains, each of which binds one copper atom (CuH and CuM). The CuM site includes Met(314) and two His residues as ligands. Mutation of Met(314) to Ile inactivates PHM, but has only a minimal effect on the EXAFS spectrum of the oxidized enzyme, implying that it contributes only marginally to stabilization of the CuM site. To characterize the role of Met(314) as a CuM ligand, we determined the structure of the Met(314)Ile-PHM mutant. Since the mutant protein failed to crystallize in the conditions of the original wild-type protein, this structure determination required finding a new crystal form. The Met(314)Ile-PHM mutant structure confirms that the mutation does not abolish CuM binding to the enzyme, but causes other structural perturbations that affect the overall stability of the enzyme and the integrity of the CuH site. To eliminate possible effects of crystal contacts, we redetermined the structure of wt-PHM in the Met(314)Ile-PHM crystal form and showed that it does not differ from the structure of wild-type (wt)-PHM in the original crystals. Met(314)Ile-PHM was also shown to be less stable than wt-PHM by differential scanning calorimetry. Both structural and calorimetric studies point to a structural role for the CuM site, in addition to its established catalytic role.
About this Structure
1YI9 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
The catalytic copper of peptidylglycine alpha-hydroxylating monooxygenase also plays a critical structural role., Siebert X, Eipper BA, Mains RE, Prigge ST, Blackburn NJ, Amzel LM, Biophys J. 2005 Nov;89(5):3312-9. Epub 2005 Aug 12. PMID:16100265
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