3phm
From Proteopedia
(New page: 200px<br /><applet load="3phm" size="450" color="white" frame="true" align="right" spinBox="true" caption="3phm, resolution 2.1Å" /> '''REDUCED (CU+) PEPTIDY...) |
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| - | [[Image:3phm.gif|left|200px]]<br /><applet load="3phm" size=" | + | [[Image:3phm.gif|left|200px]]<br /><applet load="3phm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="3phm, resolution 2.1Å" /> | caption="3phm, resolution 2.1Å" /> | ||
'''REDUCED (CU+) PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM)'''<br /> | '''REDUCED (CU+) PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Peptide amidation is a ubiquitous posttranslational modification of | + | 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== | ==About this Structure== | ||
| - | 3PHM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with CU, AZI, NI and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 3PHM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=CU:'>CU</scene>, <scene name='pdbligand=AZI:'>AZI</scene>, <scene name='pdbligand=NI:'>NI</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PHM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Amzel, L | + | [[Category: Amzel, L M.]] |
| - | [[Category: Prigge, S | + | [[Category: Prigge, S T.]] |
[[Category: AZI]] | [[Category: AZI]] | ||
[[Category: CU]] | [[Category: CU]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:11:01 2008'' |
Revision as of 17:11, 21 February 2008
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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 with , , and 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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