2ouu: Difference between revisions

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-[[Image:2ouu.gif|left|200px]]
- {{Structure
+==crystal structure of PDE10A2 mutant D674A in complex with cGMP==
-|PDB= 2ouu |SIZE=350|CAPTION= <scene name='initialview01'>2ouu</scene>, resolution 1.52&Aring;
+<StructureSection load='2ouu' size='340' side='right'caption='[[2ouu]], [[Resolution|resolution]] 1.52&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=35G:GUANOSINE-3',5'-MONOPHOSPHATE'>35G</scene>
+<table><tr><td colspan='2'>[[2ouu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OUU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OUU FirstGlance]. <br>
-|ACTIVITY= [http://en.wikipedia.org/wiki/3',5'-cyclic-nucleotide_phosphodiesterase 3',5'-cyclic-nucleotide phosphodiesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.17 3.1.4.17]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.52&#8491;</td></tr>
-|GENE= PDE10A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=35G:GUANOSINE-3,5-MONOPHOSPHATE'>35G</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=2ouu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ouu OCA], [https://pdbe.org/2ouu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ouu RCSB], [https://www.ebi.ac.uk/pdbsum/2ouu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ouu ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PDE10_HUMAN PDE10_HUMAN] Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. Can hydrolyze both cAMP and cGMP, but has higher affinity for cAMP and is more efficient with cAMP as substrate.<ref>PMID:17389385</ref>
+== 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/ou/2ouu_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=2ouu ConSurf].
+<div style="clear:both"></div>
-'''crystal structure of PDE10A2 mutant D674A in complex with cGMP'''
+==See Also==
+*[[Phosphodiesterase 3D structures|Phosphodiesterase 3D structures]]
+== References ==
-==Overview==
+<references/>
-Phosphodiesterases (PDEs) hydrolyze the second messengers cAMP and cGMP. It remains unknown how individual PDE families selectively recognize cAMP and cGMP. This work reports structural studies on substrate specificity. The crystal structures of the catalytic domains of the D674A and D564N mutants of PDE10A2 in complex with cAMP and cGMP reveal that two substrates bind to the active site with the same syn configuration but different orientations and interactions. The products AMP and GMP bind PDE10A2 with the anti configuration and interact with both divalent metals, in contrast to no direct contact of the substrates. The structures suggest that the syn configurations of cAMP and cGMP are the genuine substrates for PDE10 and the specificity is achieved through the different interactions and conformations of the substrates. The PDE10A2 structures also show that the conformation of the invariant glutamine is locked by two hydrogen bonds and is unlikely to switch for substrate recognition. Sequence alignment shows a potential pocket, in which variation of amino acids across PDE families defines the size and shape of the pocket and thus determines the substrate specificity.
+__TOC__
+</StructureSection>
-==About this Structure==
-OUU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OUU OCA].
-==Reference==
-Structural insight into substrate specificity of phosphodiesterase 10., Wang H, Liu Y, Hou J, Zheng M, Robinson H, Ke H, Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5782-7. Epub 2007 Mar 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17389385 17389385]
-[[Category: 3',5'-cyclic-nucleotide phosphodiesterase]]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Hou, J.]]
+[[Category: Hou J]]
-[[Category: Liu, Y D.]]
+[[Category: Liu YD]]
-[[Category: Robinson, H.]]
+[[Category: Robinson H]]
-[[Category: Wang, H C.]]
+[[Category: Wang HC]]
-[[Category: Zheng, M Y.]]
+[[Category: Zheng MY]]
-[[Category: 35G]]
-[[Category: MG]]
-[[Category: cgmp]]
-[[Category: pde]]
-[[Category: substrate specificity]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:04:45 2008''