1eiq: Difference between revisions

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-[[Image:1eiq.jpg|left|200px]]
- {{Structure
+==2,3-DIHYDROXYBIPHENYL-1,2-DIOXYGENASE==
-|PDB= 1eiq |SIZE=350|CAPTION= <scene name='initialview01'>1eiq</scene>, resolution 2.0&Aring;
+<StructureSection load='1eiq' size='340' side='right'caption='[[1eiq]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=FE:FE (III) ION'>FE</scene>
+<table><tr><td colspan='2'>[[1eiq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._KKS102 Pseudomonas sp. KKS102]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EIQ FirstGlance]. <br>
-|ACTIVITY= [http://en.wikipedia.org/wiki/Biphenyl-2,3-diol_1,2-dioxygenase Biphenyl-2,3-diol 1,2-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.39 1.13.11.39]
+</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>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</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=1eiq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eiq OCA], [https://pdbe.org/1eiq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eiq RCSB], [https://www.ebi.ac.uk/pdbsum/1eiq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eiq ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/BPHC_PSES1 BPHC_PSES1]
+== 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/ei/1eiq_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=1eiq ConSurf].
+<div style="clear:both"></div>
-'''2,3-DIHYDROXYBIPHENYL-1,2-DIOXYGENASE'''
+==See Also==
+*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-BphC derived from Pseudomonas sp. strain KKS102, an extradiol type catecholic dioxygenase, is a non-heam iron-containing enzyme, playing an important role in the degradation of biphenyl/PCB (Poly Chlorinated Biphenyls) in the microbe. Although we had earlier solved the crystal structure of KKS102 BphC, it was the inactive form with Fe(III) in the active site. In order to determine the active form structure, BphC was re-activated by anaerobic incubation with Fe(II) and ascorbate, and crystallized anaerobically. The crystal structures of activated BphC and its substrate complex (E x S complex) were determined at 2.0 A resolution under cryogenic condition. In addition, crystal structures of unactivated BphC in substrate free and complex forms were also re-determined. Comparison of activated and unactivated E x S complexes reveals that the orientation of the bound substrate in the active site is significantly different between the two. The structural comparison of the substrate free and complex forms of activated BphC show certain small conformational shifts around the active site upon substrate binding. As a result of the conformational shifts, His194, which has been suggested as the catalytic base, takes part in a weak hydrogen bond with hydroxyl group of the substrate.
+[[Category: Large Structures]]
+[[Category: Pseudomonas sp. KKS102]]
-==About this Structure==
+[[Category: Senda T]]
-EIQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EIQ OCA].
-==Reference==
-Crystal structures of substrate free and complex forms of reactivated BphC, an extradiol type ring-cleavage dioxygenase., Uragami Y, Senda T, Sugimoto K, Sato N, Nagarajan V, Masai E, Fukuda M, Mitsu Y, J Inorg Biochem. 2001 Feb;83(4):269-79. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11293547 11293547]
-[[Category: Biphenyl-2,3-diol 1,2-dioxygenase]]
-[[Category: Pseudomonas sp.]]
-[[Category: Single protein]]
-[[Category: Senda, T.]]
-[[Category: FE]]
-[[Category: four repetitions of beta-alpha-beta-beta-beta motif]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:56:08 2008''