1phm

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[[Image:1phm.jpg|left|200px]]
[[Image:1phm.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1phm |SIZE=350|CAPTION= <scene name='initialview01'>1phm</scene>, resolution 1.90&Aring;
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The line below this paragraph, containing "STRUCTURE_1phm", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=CUB:Active+Site+Residues+R240,Y318,N316+H+Bond+To+Peptidylgl+...'>CUB</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1phm| PDB=1phm | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1phm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1phm OCA], [http://www.ebi.ac.uk/pdbsum/1phm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1phm RCSB]</span>
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}}
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'''PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM) FROM RAT'''
'''PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM) FROM RAT'''
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[[Category: Amzel, L M.]]
[[Category: Amzel, L M.]]
[[Category: Prigge, S T.]]
[[Category: Prigge, S T.]]
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[[Category: ascorbate]]
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[[Category: Ascorbate]]
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[[Category: bioactive peptide activation]]
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[[Category: Bioactive peptide activation]]
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[[Category: copper]]
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[[Category: Copper]]
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[[Category: monooxygenase]]
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[[Category: Monooxygenase]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:05:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:59:48 2008''
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Revision as of 02:05, 3 May 2008

Image:1phm.jpg

Template:STRUCTURE 1phm

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 Sat May 3 05:05:41 2008

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