1py0: Difference between revisions

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-[[Image:1py0.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1py0", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
--->
-{{STRUCTURE_1py0|  PDB=1py0  |  SCENE=  }}
-'''Crystal structure of E51C/E54C Psaz from A.faecalis with CLaNP probe'''
+==Crystal structure of E51C/E54C Psaz from A.faecalis with CLaNP probe==
+<StructureSection load='1py0' size='340' side='right'caption='[[1py0]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1py0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PY0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PY0 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&#8491;</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>, <scene name='pdbligand=Y1:YTTRIUM+ION'>Y1</scene>, <scene name='pdbligand=YMA:7,10,13-TRI(CARBOXYMETHYL)-5,15-DIOXO-4,7,10,13,16-PENTAAZA-1,19-DITHIANONADECANE'>YMA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1py0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1py0 OCA], [https://pdbe.org/1py0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1py0 RCSB], [https://www.ebi.ac.uk/pdbsum/1py0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1py0 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/AZUP_ALCFA AZUP_ALCFA] This soluble electron transfer copper protein is required for the inactivation of copper-containing nitrite reductase in the presence of oxygen. Serves as a direct electron donor to the nitrite reductase.
+== 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/py/1py0_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1py0 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A lanthanide complex, named CLaNP (caged lanthanide NMR probe) has been developed for the characterisation of proteins by paramagnetic NMR spectroscopy. The probe consists of a lanthanide chelated by a derivative of DTPA (diethylenetriaminepentaacetic acid) with two thiol reactive functional groups. The CLaNP molecule is attached to a protein by two engineered, surface-exposed, Cys residues in a bidentate manner. This drastically limits the dynamics of the metal relative to the protein and enables measurements of pseudocontact shifts. NMR spectroscopy experiments on a diamagnetic control and the crystal structure of the probe-protein complex demonstrate that the protein structure is not affected by probe attachment. The probe is able to induce pseudocontact shifts to at least 40 A from the metal and causes residual dipolar couplings due to alignment at a high magnetic field. The molecule exists in several isomeric forms with different paramagnetic tensors; this provides a fast way to obtain long-range distance restraints.
-==Overview==
+A caged lanthanide complex as a paramagnetic shift agent for protein NMR.,Prudencio M, Rohovec J, Peters JA, Tocheva E, Boulanger MJ, Murphy ME, Hupkes HJ, Kosters W, Impagliazzo A, Ubbink M Chemistry. 2004 Jul 5;10(13):3252-60. PMID:15224334<ref>PMID:15224334</ref>
-A lanthanide complex, named CLaNP (caged lanthanide NMR probe) has been developed for the characterisation of proteins by paramagnetic NMR spectroscopy. The probe consists of a lanthanide chelated by a derivative of DTPA (diethylenetriaminepentaacetic acid) with two thiol reactive functional groups. The CLaNP molecule is attached to a protein by two engineered, surface-exposed, Cys residues in a bidentate manner. This drastically limits the dynamics of the metal relative to the protein and enables measurements of pseudocontact shifts. NMR spectroscopy experiments on a diamagnetic control and the crystal structure of the probe-protein complex demonstrate that the protein structure is not affected by probe attachment. The probe is able to induce pseudocontact shifts to at least 40 A from the metal and causes residual dipolar couplings due to alignment at a high magnetic field. The molecule exists in several isomeric forms with different paramagnetic tensors; this provides a fast way to obtain long-range distance restraints.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-PY0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PY0 OCA].
+</div>
+<div class="pdbe-citations 1py0" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-A caged lanthanide complex as a paramagnetic shift agent for protein NMR., Prudencio M, Rohovec J, Peters JA, Tocheva E, Boulanger MJ, Murphy ME, Hupkes HJ, Kosters W, Impagliazzo A, Ubbink M, Chemistry. 2004 Jul 5;10(13):3252-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15224334 15224334]
+*[[Pseudoazurin|Pseudoazurin]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Alcaligenes faecalis]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Boulanger, M J.]]
+[[Category: Boulanger MJ]]
-[[Category: Hupkes, H J.]]
+[[Category: Hupkes HJ]]
-[[Category: Impagliazzo, A.]]
+[[Category: Impagliazzo A]]
-[[Category: Kosters, W.]]
+[[Category: Kosters W]]
-[[Category: Murphy, M E.]]
+[[Category: Murphy ME]]
-[[Category: Peters, J A.]]
+[[Category: Peters JA]]
-[[Category: Prudencio, M.]]
+[[Category: Prudencio M]]
-[[Category: Rohovec, J.]]
+[[Category: Rohovec J]]
-[[Category: Tocheva, E.]]
+[[Category: Tocheva E]]
-[[Category: Ubbink, M.]]
+[[Category: Ubbink M]]
-[[Category: Cupredoxin]]
-[[Category: Nmr probe]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:37:46 2008''