1yip

From Proteopedia

(Difference between revisions)

Current revision

Oxidized Peptidylglycine Alpha-Hydroxylating Monooxygenase (PHM) in a New Crystal Form

Structural highlights

1yip is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.2Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AMD_RAT Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Many bioactive peptides require amidation of their carboxy terminus to exhibit full biological activity. Peptidylglycine alpha-hydroxylating monooxygenase (PHM; EC 1.14.17.3), the enzyme that catalyzes the first of the two steps of this reaction, is composed of two domains, each of which binds one copper atom (CuH and CuM). The CuM site includes Met(314) and two His residues as ligands. Mutation of Met(314) to Ile inactivates PHM, but has only a minimal effect on the EXAFS spectrum of the oxidized enzyme, implying that it contributes only marginally to stabilization of the CuM site. To characterize the role of Met(314) as a CuM ligand, we determined the structure of the Met(314)Ile-PHM mutant. Since the mutant protein failed to crystallize in the conditions of the original wild-type protein, this structure determination required finding a new crystal form. The Met(314)Ile-PHM mutant structure confirms that the mutation does not abolish CuM binding to the enzyme, but causes other structural perturbations that affect the overall stability of the enzyme and the integrity of the CuH site. To eliminate possible effects of crystal contacts, we redetermined the structure of wt-PHM in the Met(314)Ile-PHM crystal form and showed that it does not differ from the structure of wild-type (wt)-PHM in the original crystals. Met(314)Ile-PHM was also shown to be less stable than wt-PHM by differential scanning calorimetry. Both structural and calorimetric studies point to a structural role for the CuM site, in addition to its established catalytic role.

The catalytic copper of peptidylglycine alpha-hydroxylating monooxygenase also plays a critical structural role.,Siebert X, Eipper BA, Mains RE, Prigge ST, Blackburn NJ, Amzel LM Biophys J. 2005 Nov;89(5):3312-9. Epub 2005 Aug 12. PMID:16100265^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Siebert X, Eipper BA, Mains RE, Prigge ST, Blackburn NJ, Amzel LM. The catalytic copper of peptidylglycine alpha-hydroxylating monooxygenase also plays a critical structural role. Biophys J. 2005 Nov;89(5):3312-9. Epub 2005 Aug 12. PMID:16100265 doi:10.1529/biophysj.105.066100

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1yip"

@@ Line 1: / Line 1: @@
 ==Oxidized Peptidylglycine Alpha-Hydroxylating Monooxygenase (PHM) in a New Crystal Form==
-<StructureSection load='1yip' size='340' side='right' caption='[[1yip]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+<StructureSection load='1yip' size='340' side='right'caption='[[1yip]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1yip]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YIP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YIP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1yip]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YIP FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yi9|1yi9]], [[1phm|1phm]], [[1opm|1opm]], [[3phm|3phm]], [[1sdw|1sdw]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Pam ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yip OCA], [https://pdbe.org/1yip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yip RCSB], [https://www.ebi.ac.uk/pdbsum/1yip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yip ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yip OCA], [http://pdbe.org/1yip PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yip RCSB], [http://www.ebi.ac.uk/pdbsum/1yip PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/AMD_RAT AMD_RAT]] Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
+[https://www.uniprot.org/uniprot/AMD_RAT AMD_RAT] Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yi/1yip_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yi/1yip_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 30: / Line 29: @@
 </div>
 <div class="pdbe-citations 1yip" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Buffalo rat]]
+[[Category: Large Structures]]
-[[Category: Peptidylglycine monooxygenase]]
+[[Category: Rattus norvegicus]]
-[[Category: Amzel, L M]]
+[[Category: Amzel LM]]
-[[Category: Blackburn, N J]]
+[[Category: Blackburn NJ]]
-[[Category: Eipper, B A]]
+[[Category: Eipper BA]]
-[[Category: Mains, R E]]
+[[Category: Mains RE]]
-[[Category: Prigge, S T]]
+[[Category: Prigge ST]]
-[[Category: Siebert, X]]
+[[Category: Siebert X]]
-[[Category: Ascorbate]]
-[[Category: Bioactive peptide activation]]
-[[Category: Monooxygenase]]
-[[Category: Oxidoreductase]]

1yip

From Proteopedia

Current revision

Oxidized Peptidylglycine Alpha-Hydroxylating Monooxygenase (PHM) in a New Crystal Form

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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