1jr4: Difference between revisions

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New page: left|200px<br /><applet load="1jr4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jr4, resolution 2.63Å" /> '''CATECHOL O-METHYLTRA...
 
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[[Image:1jr4.jpg|left|200px]]<br /><applet load="1jr4" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1jr4, resolution 2.63&Aring;" />
'''CATECHOL O-METHYLTRANSFERASE BISUBSTRATE-INHIBITOR COMPLEX'''<br />


==About this Structure==
==CATECHOL O-METHYLTRANSFERASE BISUBSTRATE-INHIBITOR COMPLEX==
1JR4 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 MG and CL4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Catechol_O-methyltransferase Catechol O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.6 2.1.1.6] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JR4 OCA].  
<StructureSection load='1jr4' size='340' side='right'caption='[[1jr4]], [[Resolution|resolution]] 2.63&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1jr4]] 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=1JR4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JR4 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.63&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL4:N-{3-[5-(6-AMINO-PURIN-9-YL)-3,4-DIHYDROXY-TETRAHYDRO-FURAN-2-YL]-ALLYL}-2,3-DIHYDROXY-5-NITRO-BENZAMIDE'>CL4</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=1jr4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jr4 OCA], [https://pdbe.org/1jr4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jr4 RCSB], [https://www.ebi.ac.uk/pdbsum/1jr4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jr4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/COMT_RAT COMT_RAT] Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol.
== 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/jr/1jr4_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jr4 ConSurf].
<div style="clear:both"></div>


==Reference==
==See Also==
X-ray Crystal Structure of a Bisubstrate Inhibitor Bound to the Enzyme Catechol-O-methyltransferase: A Dramatic Effect of Inhibitor Preorganization on Binding Affinity We thank F. Hoffmann-La Roche for generous support of this work. We are grateful to P. Malherbe for the cloning of COMT, P. Caspers for the expression of COMT, A. Cesura for enzyme purification, B. Wipf for fermentation, and H. W. Lahm for sequencing. , Lerner C, Ruf A, Gramlich V, Masjost B, Zurcher G, Jakob-Roetne R, Borroni E, Diederich F, Angew Chem Int Ed Engl. 2001 Nov 5;40(21):4040-4042. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12404486 12404486]
*[[Catechol O-methyltransferase 3D structures|Catechol O-methyltransferase 3D structures]]
[[Category: Catechol O-methyltransferase]]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Ruf A]]
[[Category: Ruf, A.]]
[[Category: Stihle M]]
[[Category: Stihle, M.]]
[[Category: CL4]]
[[Category: MG]]
[[Category: bisubstrate inhibitor]]
[[Category: methyltransferase]]
[[Category: neurotransmitter degradation]]
[[Category: transferase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:30:27 2007''

Latest revision as of 10:41, 7 February 2024

CATECHOL O-METHYLTRANSFERASE BISUBSTRATE-INHIBITOR COMPLEXCATECHOL O-METHYLTRANSFERASE BISUBSTRATE-INHIBITOR COMPLEX

Structural highlights

1jr4 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 2.63Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

COMT_RAT Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol.

Evolutionary Conservation

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

See Also

1jr4, resolution 2.63Å

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