2zlb

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of APO form of rat catechol-O-methyltransferase

Structural highlights

2zlb 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

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.

Publication Abstract from PubMed

Catechol-O-methyltransferase (COMT, EC 2.1.1.6) is a monomeric enzyme that catalyzes the transfer of a methyl group from S-adenosyl-l-methionine (AdoMet) to the phenolic oxygen of substituted catechols. Although the inhibitor recognition pattern and AdoMet site have already been studied crystallographically, structural information on the catalytic cycle of COMT has not yet been obtained. In this study, comparison of the co-factor and inhibitor-bound structures revealed that the Apo form of COMT shows a conformational change and there was no cleft corresponding to the AdoMet-binding site; the overall structure was partially open form and the substrate recognition site was not clearly defined. The Holo form of COMT was similar to the quaternary structure except for the beta6-beta7 and alpha2-alpha3 ligand recognition loops. These conformational changes provide a deeper insight into the structural events occurring in reactions catalyzed by AdoMet.

Crystal structures of the Apo and Holo form of rat catechol-O-methyltransferase.,Tsuji E, Okazaki K, Isaji M, Takeda K J Struct Biol. 2008 Dec 10. PMID:19111934^[1]

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

References

↑ Tsuji E, Okazaki K, Isaji M, Takeda K. Crystal structures of the Apo and Holo form of rat catechol-O-methyltransferase. J Struct Biol. 2008 Dec 10. PMID:19111934 doi:S1047-8477(08)00293-1

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/2zlb"

Categories: Large Structures | Rattus norvegicus | Tsuji E

@@ Line 3: / Line 3: @@
 <StructureSection load='2zlb' size='340' side='right'caption='[[2zlb]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2zlb]] 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=2ZLB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2ZLB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2zlb]] 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=2ZLB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZLB FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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">[[1vid|1vid]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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=2zlb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zlb OCA], [https://pdbe.org/2zlb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zlb RCSB], [https://www.ebi.ac.uk/pdbsum/2zlb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zlb ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2zlb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zlb OCA], [http://pdbe.org/2zlb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zlb RCSB], [http://www.ebi.ac.uk/pdbsum/2zlb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zlb ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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.
+[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]]
@@ Line 37: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Buffalo rat]]
-[[Category: Catechol O-methyltransferase]]
 [[Category: Large Structures]]
-[[Category: Tsuji, E]]
+[[Category: Rattus norvegicus]]
-[[Category: Alternative initiation]]
+[[Category: Tsuji E]]
-[[Category: Catecholamine metabolism]]
-[[Category: Cytoplasm]]
-[[Category: Magnesium]]
-[[Category: Membrane]]
-[[Category: Metal-binding]]
-[[Category: Methyltransferase]]
-[[Category: Neurotransmitter degradation]]
-[[Category: Phosphoprotein]]
-[[Category: S-adenosyl-l-methionine]]
-[[Category: Signal-anchor]]
-[[Category: Transferase]]
-[[Category: Transmembrane]]

2zlb

From Proteopedia

Current revision

Crystal structure of APO form of rat catechol-O-methyltransferase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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