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2j55
From Proteopedia
(Difference between revisions)
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| - | [[ | + | ==X-RAY REDUCED PARACCOCUS DENITRIFICANS METHYLAMINE DEHYDROGENASE O-QUINONE IN COMPLEX WITH AMICYANIN.== |
| + | <StructureSection load='2j55' size='340' side='right' caption='[[2j55]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2j55]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J55 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2J55 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1aac|1aac]], [[1aaj|1aaj]], [[1aan|1aan]], [[1bxa|1bxa]], [[1mda|1mda]], [[1mg2|1mg2]], [[1mg3|1mg3]], [[1sf3|1sf3]], [[1sf5|1sf5]], [[1sfd|1sfd]], [[1sfh|1sfh]], [[1t5k|1t5k]], [[2mta|2mta]], [[2rac|2rac]], [[2bbk|2bbk]], [[2j56|2j56]], [[2j57|2j57]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Amine_dehydrogenase Amine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.99.3 1.4.99.3] </span></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=2j55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j55 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2j55 RCSB], [http://www.ebi.ac.uk/pdbsum/2j55 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/AMCY_PARDE AMCY_PARDE]] Primary acceptor of electrons from methylamine dehydrogenase. Passes those electrons on either a soluble cytochrome c or to pseudoazurin. [[http://www.uniprot.org/uniprot/DHML_PARDE DHML_PARDE]] Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin. [[http://www.uniprot.org/uniprot/DHMH_PARDE DHMH_PARDE]] Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin. | ||
| + | == 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/j5/2j55_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 == | ||
| + | X-ray exposure during crystallographic data collection can result in unintended redox changes in proteins containing functionally important redox centers. In order to directly monitor X-ray-derived redox changes in trapped oxidative half-reaction intermediates of Paracoccus denitrificans methylamine dehydrogenase, a commercially available single-crystal UV/Vis microspectrophotometer was installed on-line at the BioCARS beamline 14-BM-C at the Advanced Photon Source, Argonne, USA. Monitoring the redox state of the intermediates during X-ray exposure permitted the creation of a general multi-crystal data collection strategy to generate true structures of each redox intermediate. | ||
| - | + | Tracking X-ray-derived redox changes in crystals of a methylamine dehydrogenase/amicyanin complex using single-crystal UV/Vis microspectrophotometry.,Pearson AR, Pahl R, Kovaleva EG, Davidson VL, Wilmot CM J Synchrotron Radiat. 2007 Jan;14(Pt 1):92-8. Epub 2006 Dec 15. PMID:17211075<ref>PMID:17211075</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
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| - | + | ||
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| - | + | ||
==See Also== | ==See Also== | ||
*[[Methylamine dehydrogenase|Methylamine dehydrogenase]] | *[[Methylamine dehydrogenase|Methylamine dehydrogenase]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Amine dehydrogenase]] | [[Category: Amine dehydrogenase]] | ||
[[Category: Paracoccus denitrificans]] | [[Category: Paracoccus denitrificans]] | ||
| - | [[Category: Davidson, V L | + | [[Category: Davidson, V L]] |
| - | [[Category: Pahl, R | + | [[Category: Pahl, R]] |
| - | [[Category: Pearson, A R | + | [[Category: Pearson, A R]] |
| - | [[Category: Wilmot, C M | + | [[Category: Wilmot, C M]] |
[[Category: Electron transport]] | [[Category: Electron transport]] | ||
[[Category: Metal-binding]] | [[Category: Metal-binding]] | ||
Revision as of 18:52, 25 December 2014
X-RAY REDUCED PARACCOCUS DENITRIFICANS METHYLAMINE DEHYDROGENASE O-QUINONE IN COMPLEX WITH AMICYANIN.
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