2j57

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[[Image:2j57.gif|left|200px]]
 
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{{Structure
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==X-ray reduced Paraccocus denitrificans methylamine dehydrogenase N- quinol in complex with amicyanin.==
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|PDB= 2j57 |SIZE=350|CAPTION= <scene name='initialview01'>2j57</scene>, resolution 2.25&Aring;
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<StructureSection load='2j57' size='340' side='right'caption='[[2j57]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Cu+Binding+Site+For+Chain+D'>AC1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=TQQ:(S)-2-AMINO-3-(6,7-DIHYDRO-6-IMINO-7-OXO-1H-INDOL-3-YL)PROPANOIC+ACID'>TQQ</scene>
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<table><tr><td colspan='2'>[[2j57]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J57 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J57 FirstGlance]. <br>
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|ACTIVITY= <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>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
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|GENE=
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TQQ:(S)-2-AMINO-3-(6,7-DIHYDRO-6-IMINO-7-OXO-1H-INDOL-3-YL)PROPANOIC+ACID'>TQQ</scene></td></tr>
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|DOMAIN=
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[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]], [[2j55|2j55]], [[2j56|2j56]]</div></td></tr>
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|RELATEDENTRY=
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Methylamine_dehydrogenase_(amicyanin) Methylamine dehydrogenase (amicyanin)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.9.1 1.4.9.1] </span></td></tr>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j57 OCA], [http://www.ebi.ac.uk/pdbsum/2j57 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2j57 RCSB]</span>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2j57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j57 OCA], [https://pdbe.org/2j57 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j57 RCSB], [https://www.ebi.ac.uk/pdbsum/2j57 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j57 ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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[[https://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. [[https://www.uniprot.org/uniprot/DHML_PARDE DHML_PARDE]] Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin. [[https://www.uniprot.org/uniprot/DHMH_PARDE DHMH_PARDE]] Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j5/2j57_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2j57 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''X-RAY REDUCED PARACCOCUS DENITRIFICANS METHYLAMINE DEHYDROGENASE N-QUINOL IN COMPLEX WITH AMICYANIN.'''
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2j57" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Methylamine dehydrogenase|Methylamine dehydrogenase]]
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== References ==
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==About this Structure==
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<references/>
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2J57 is a [[Protein complex]] structure of sequences 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=2J57 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17211075 17211075]
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[[Category: Amine dehydrogenase]]
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[[Category: Paracoccus denitrificans]]
[[Category: Paracoccus denitrificans]]
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[[Category: Protein complex]]
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[[Category: Davidson, V L]]
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[[Category: Davidson, V.]]
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[[Category: Pahl, R]]
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[[Category: Pahl, R.]]
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[[Category: Pearson, A R]]
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[[Category: Pearson, A R.]]
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[[Category: Wilmot, C M]]
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[[Category: Wilmot, C M.]]
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[[Category: Electron transport]]
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[[Category: copper]]
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[[Category: Metal-binding]]
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[[Category: electron transport]]
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[[Category: Oxidoreductase]]
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[[Category: metal-binding]]
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[[Category: Periplasmic]]
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[[Category: methylamine dehydrogenase single crystal microspectrophoto]]
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[[Category: Single crystal microspectrophotometry]]
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[[Category: oxidoreductase]]
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[[Category: periplasmic]]
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[[Category: transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:53:08 2008''
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Current revision

X-ray reduced Paraccocus denitrificans methylamine dehydrogenase N- quinol in complex with amicyanin.

PDB ID 2j57

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