3dhh
From Proteopedia
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- | [[ | + | ==Crystal Structure of Resting State Toluene 4-Monoxygenase Hydroxylase Complexed with Effector Protein== |
+ | <StructureSection load='3dhh' size='340' side='right' caption='[[3dhh]], [[Resolution|resolution]] 1.94Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3dhh]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_mendocina Pseudomonas mendocina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DHH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DHH FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=BML:4-BROMOPHENOL'>BML</scene>, <scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tmoA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300 Pseudomonas mendocina]), tmoE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300 Pseudomonas mendocina]), tmoB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300 Pseudomonas mendocina]), tmoD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300 Pseudomonas mendocina])</td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3dhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dhh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dhh RCSB], [http://www.ebi.ac.uk/pdbsum/3dhh PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == 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/dh/3dhh_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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Carboxylate-bridged diiron hydroxylases are multicomponent enzyme complexes responsible for the catabolism of a wide range of hydrocarbons and as such have drawn attention for their mechanism of action and potential uses in bioremediation and enzymatic synthesis. These enzyme complexes use a small molecular weight effector protein to modulate the function of the hydroxylase. However, the origin of these functional changes is poorly understood. Here, we report the structures of the biologically relevant effector protein-hydroxylase complex of toluene 4-monooxygenase in 2 redox states. The structures reveal a number of coordinated changes that occur up to 25 A from the active site and poise the diiron center for catalysis. The results provide a structural basis for the changes observed in a number of the measurable properties associated with effector protein binding. This description provides insight into the functional role of effector protein binding in all carboxylate-bridged diiron hydroxylases. | ||
- | + | Structural consequences of effector protein complex formation in a diiron hydroxylase.,Bailey LJ, McCoy JG, Phillips GN Jr, Fox BG Proc Natl Acad Sci U S A. 2008 Dec 9;105(49):19194-8. Epub 2008 Nov 25. PMID:19033467<ref>PMID:19033467</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
+ | </div> | ||
- | + | ==See Also== | |
- | + | *[[Monooxygenase|Monooxygenase]] | |
- | == | + | == References == |
- | [[ | + | <references/> |
- | + | __TOC__ | |
- | == | + | </StructureSection> |
- | < | + | |
[[Category: Pseudomonas mendocina]] | [[Category: Pseudomonas mendocina]] | ||
- | [[Category: Bailey, L J | + | [[Category: Bailey, L J]] |
- | [[Category: Fox, B G | + | [[Category: Fox, B G]] |
- | [[Category: Mccoy, J G | + | [[Category: Mccoy, J G]] |
- | [[Category: Phillips, G N | + | [[Category: Phillips, G N]] |
[[Category: Aromatic hydrocarbons catabolism]] | [[Category: Aromatic hydrocarbons catabolism]] | ||
[[Category: Fad]] | [[Category: Fad]] |
Revision as of 08:05, 12 November 2014
Crystal Structure of Resting State Toluene 4-Monoxygenase Hydroxylase Complexed with Effector Protein
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