3phm
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:3phm.gif|left|200px]] | + | [[Image:3phm.gif|left|200px]] |
| - | + | ||
| - | '''REDUCED (CU+) PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM)''' | + | {{Structure |
| + | |PDB= 3phm |SIZE=350|CAPTION= <scene name='initialview01'>3phm</scene>, resolution 2.1Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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= | ||
| + | }} | ||
| + | |||
| + | '''REDUCED (CU+) PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM)''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 3PHM is a [ | + | 3PHM 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=3PHM OCA]. |
==Reference== | ==Reference== | ||
| - | Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase., Prigge ST, Kolhekar AS, Eipper BA, Mains RE, Amzel LM, Nat Struct Biol. 1999 Oct;6(10):976-83. PMID:[http:// | + | Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase., Prigge ST, Kolhekar AS, Eipper BA, Mains RE, Amzel LM, Nat Struct Biol. 1999 Oct;6(10):976-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10504734 10504734] |
[[Category: Peptidylglycine monooxygenase]] | [[Category: Peptidylglycine monooxygenase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
| Line 26: | Line 35: | ||
[[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 19:06:41 2008'' |
Revision as of 17:06, 20 March 2008
| |||||||
| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , and | ||||||
| Activity: | Peptidylglycine monooxygenase, with EC number 1.14.17.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
REDUCED (CU+) PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM)
Overview
Peptide amidation is a ubiquitous posttranslational modification of bioactive peptides. Peptidylglycine alpha-hydroxylating monooxygenase (PHM; EC 1.14.17.3), the enzyme that catalyzes the first step of this reaction, is composed of two domains, each of which binds one copper atom. The coppers are held 11 A apart on either side of a solvent-filled interdomain cleft, and the PHM reaction requires electron transfer between these sites. A plausible mechanism for electron transfer might involve interdomain motion to decrease the distance between the copper atoms. Our experiments show that PHM catalytic core (PHMcc) is enzymatically active in the crystal phase, where interdomain motion is not possible. Instead, structures of two states relevant to catalysis indicate that water, substrate and active site residues may provide an electron transfer pathway that exists only during the PHM catalytic cycle.
About this Structure
3PHM is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase., Prigge ST, Kolhekar AS, Eipper BA, Mains RE, Amzel LM, Nat Struct Biol. 1999 Oct;6(10):976-83. PMID:10504734
Page seeded by OCA on Thu Mar 20 19:06:41 2008
