1opm

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Revision as of 20:58, 20 November 2007

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spinqualitylabelsall models 1opm, resolution 2.1Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

OXIDIZED (CU2+) PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM) WITH BOUND SUBSTRATE

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

1OPM is a Single protein structure of sequence from Rattus norvegicus with CU, AZI, NI, IYG and GOL as ligands. Active as Peptidylglycine monooxygenase, with EC number 1.14.17.3 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

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