1mda

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(New page: 200px<br /><applet load="1mda" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mda, resolution 2.5&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1mda.gif|left|200px]]<br /><applet load="1mda" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mda, resolution 2.5&Aring;" />
 
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'''CRYSTAL STRUCTURE OF AN ELECTRON-TRANSFER COMPLEX BETWEEN METHYLAMINE DEHYDROGENASE AND AMICYANIN'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF AN ELECTRON-TRANSFER COMPLEX BETWEEN METHYLAMINE DEHYDROGENASE AND AMICYANIN==
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The crystal structure of the complex between the quinoprotein methylamine, dehydrogenase (MADH) and the type I blue copper protein amicyanin, both, from Paracoccus denitrificans, has been determined at 2.5-A resolution, using molecular replacement. The search model was MADH from Thiobacillus, versutus. The amicyanin could be located in an averaged electron density, difference map and the model improved by refinement and model building, procedures. Nine beta-strands are observed within the amicyanin molecule., The copper atom is located between three antiparallel strands and is about, 2.5 A below the protein surface. The major intermolecular interactions, occur between amicyanin and the light subunit of MADH where the interface, is largely hydrophobic. The copper atom of amicyanin and the redox, cofactor of MADH are about 9.4 A apart. One of the copper ligands, His 95, lies between the two redox centers and may facilitate electron transfer, between them.
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<StructureSection load='1mda' size='340' side='right'caption='[[1mda]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1mda]] 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=1MDA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MDA FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<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=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</scene></td></tr>
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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=1mda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mda OCA], [https://pdbe.org/1mda PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mda RCSB], [https://www.ebi.ac.uk/pdbsum/1mda PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mda ProSAT]</span></td></tr>
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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.
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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/md/1mda_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=1mda 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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The crystal structure of the complex between the quinoprotein methylamine dehydrogenase (MADH) and the type I blue copper protein amicyanin, both from Paracoccus denitrificans, has been determined at 2.5-A resolution using molecular replacement. The search model was MADH from Thiobacillus versutus. The amicyanin could be located in an averaged electron density difference map and the model improved by refinement and model building procedures. Nine beta-strands are observed within the amicyanin molecule. The copper atom is located between three antiparallel strands and is about 2.5 A below the protein surface. The major intermolecular interactions occur between amicyanin and the light subunit of MADH where the interface is largely hydrophobic. The copper atom of amicyanin and the redox cofactor of MADH are about 9.4 A apart. One of the copper ligands, His 95, lies between the two redox centers and may facilitate electron transfer between them.
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==About this Structure==
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Crystal structure of an electron-transfer complex between methylamine dehydrogenase and amicyanin.,Chen L, Durley R, Poliks BJ, Hamada K, Chen Z, Mathews FS, Davidson VL, Satow Y, Huizinga E, Vellieux FM, et al. Biochemistry. 1992 Jun 2;31(21):4959-64. PMID:1599920<ref>PMID:1599920</ref>
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1MDA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans] with CU as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MDA OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of an electron-transfer complex between methylamine dehydrogenase and amicyanin., Chen L, Durley R, Poliks BJ, Hamada K, Chen Z, Mathews FS, Davidson VL, Satow Y, Huizinga E, Vellieux FM, et al., Biochemistry. 1992 Jun 2;31(21):4959-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1599920 1599920]
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</div>
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[[Category: Amine dehydrogenase]]
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<div class="pdbe-citations 1mda" style="background-color:#fffaf0;"></div>
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[[Category: Paracoccus denitrificans]]
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[[Category: Protein complex]]
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[[Category: Chen, L.]]
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[[Category: Durley, R.]]
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[[Category: Mathews, F.S.]]
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[[Category: CU]]
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[[Category: electron transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:20:31 2007''
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==See Also==
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*[[Amicyanin 3D structures|Amicyanin 3D structures]]
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*[[Methylamine dehydrogenase|Methylamine dehydrogenase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Paracoccus denitrificans]]
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[[Category: Chen L]]
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[[Category: Durley R]]
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[[Category: Mathews FS]]

Current revision

CRYSTAL STRUCTURE OF AN ELECTRON-TRANSFER COMPLEX BETWEEN METHYLAMINE DEHYDROGENASE AND AMICYANIN

PDB ID 1mda

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