1phm
From Proteopedia
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| , resolution 1.90Å | |||||||
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| Sites: | |||||||
| Ligands: | , , | ||||||
| Activity: | Peptidylglycine monooxygenase, with EC number 1.14.17.3 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM) FROM RAT
Overview
Many neuropeptides and peptide hormones require amidation at the carboxyl terminus for activity. Peptidylglycine alpha-amidating monooxygenase (PAM) catalyzes the amidation of these diverse physiological regulators. The amino-terminal domain of the bifunctional PAM protein is a peptidylglycine alpha-hydroxylating monooxygenase (PHM) with two coppers that cycle through cupric and cuprous oxidation states. The anomalous signal of the endogenous coppers was used to determine the structure of the catalytic core of oxidized rat PHM with and without bound peptide substrate. These structures strongly suggest that the PHM reaction proceeds via activation of substrate by a copper-bound oxygen species. The mechanistic and structural insight gained from the PHM structures can be directly extended to dopamine beta-monooxygenase.
About this Structure
1PHM is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Amidation of bioactive peptides: the structure of peptidylglycine alpha-hydroxylating monooxygenase., Prigge ST, Kolhekar AS, Eipper BA, Mains RE, Amzel LM, Science. 1997 Nov 14;278(5341):1300-5. PMID:9360928
Page seeded by OCA on Sun Mar 30 22:59:48 2008
