2j55: Difference between revisions

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[[Image:2j55.gif|left|200px]]


{{Structure
==X-ray reduced Paraccocus denitrificans methylamine dehydrogenase O- quinone in complex with amicyanin.==
|PDB= 2j55 |SIZE=350|CAPTION= <scene name='initialview01'>2j55</scene>, resolution 2.15&Aring;
<StructureSection load='2j55' size='340' side='right'caption='[[2j55]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+L'>AC1</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</scene>
<table><tr><td colspan='2'>[[2j55]] is a 6 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=2J55 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J55 FirstGlance]. <br>
|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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
|GENE=
<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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2j55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j55 OCA], [https://pdbe.org/2j55 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j55 RCSB], [https://www.ebi.ac.uk/pdbsum/2j55 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j55 ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<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.ebi.ac.uk/pdbsum/2j55 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2j55 RCSB]</span>
== Function ==
}}
[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.
== 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/main_output.php?pdb_ID=2j55 ConSurf].
<div style="clear:both"></div>


'''X-RAY REDUCED PARACCOCUS DENITRIFICANS METHYLAMINE DEHYDROGENASE O-QUINONE IN COMPLEX WITH AMICYANIN.'''
==See Also==
 
*[[Amicyanin 3D structures|Amicyanin 3D structures]]
 
*[[Methylamine dehydrogenase|Methylamine dehydrogenase]]
==Overview==
__TOC__
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.
</StructureSection>
 
[[Category: Large Structures]]
==About this Structure==
2J55 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=2J55 OCA].
 
==Reference==
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]
[[Category: Amine dehydrogenase]]
[[Category: Paracoccus denitrificans]]
[[Category: Paracoccus denitrificans]]
[[Category: Protein complex]]
[[Category: Davidson VL]]
[[Category: Davidson, V.]]
[[Category: Pahl R]]
[[Category: Pahl, R.]]
[[Category: Pearson AR]]
[[Category: Pearson, A R.]]
[[Category: Wilmot CM]]
[[Category: Wilmot, C M.]]
[[Category: copper]]
[[Category: electron transport]]
[[Category: metal-binding]]
[[Category: methylamine dehydrogenase single crystal microspectrophoto]]
[[Category: oxidoreductase]]
[[Category: periplasmic]]
[[Category: transport]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:53:03 2008''

Latest revision as of 09:41, 1 May 2024

X-ray reduced Paraccocus denitrificans methylamine dehydrogenase O- quinone in complex with amicyanin.X-ray reduced Paraccocus denitrificans methylamine dehydrogenase O- quinone in complex with amicyanin.

Structural highlights

2j55 is a 6 chain structure with sequence from Paracoccus denitrificans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.15Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AMCY_PARDE Primary acceptor of electrons from methylamine dehydrogenase. Passes those electrons on either a soluble cytochrome c or to pseudoazurin.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2j55, resolution 2.15Å

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OCA
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