2gc7: Difference between revisions

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New page: left|200px<br /><applet load="2gc7" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gc7, resolution 1.90Å" /> '''Substrate reduced, c...
 
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'''Substrate reduced, copper free complex of methylamine dehydrogenase, amicyanin and cytochrome c551i from Paracoccus denitrificans.'''<br />


==Overview==
==Substrate reduced, copper free complex of methylamine dehydrogenase, amicyanin and cytochrome c551i from Paracoccus denitrificans.==
The crystal structure of a ternary protein complex has been determined at, 2.4 angstrom resolution. The complex is composed of three electron, transfer proteins from Paracoccus denitrificans, the quinoprotein, methylamine dehydrogenase, the blue copper protein amicyanin, and the, cytochrome c551i. The central region of the c551i is folded similarly to, several small bacterial c-type cytochromes; there is a 45-residue, extension at the amino terminus and a 25-residue extension at the carboxyl, terminus. The methylamine dehydrogenase-amicyanin interface is largely, hydrophobic, whereas the amicyanin-cytochrome interface is more polar, with several charged groups present on each surface. Analysis of the, simplest electron transfer pathways between the redox partners points out, the importance of other factors such as energetics in determining the, electron transfer rates.
<StructureSection load='2gc7' size='340' side='right'caption='[[2gc7]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2gc7]] is a 16 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=2GC7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GC7 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gc7 OCA], [https://pdbe.org/2gc7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gc7 RCSB], [https://www.ebi.ac.uk/pdbsum/2gc7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gc7 ProSAT]</span></td></tr>
</table>
== Function ==
[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.
== 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/gc/2gc7_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=2gc7 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2GC7 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 NA and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. 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=2GC7 OCA].
*[[Amicyanin 3D structures|Amicyanin 3D structures]]
 
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
==Reference==
*[[Methylamine dehydrogenase|Methylamine dehydrogenase]]
Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i., Chen L, Durley RC, Mathews FS, Davidson VL, Science. 1994 Apr 1;264(5155):86-90. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8140419 8140419]
__TOC__
[[Category: Amine dehydrogenase]]
</StructureSection>
[[Category: Large Structures]]
[[Category: Paracoccus denitrificans]]
[[Category: Paracoccus denitrificans]]
[[Category: Protein complex]]
[[Category: Chen Z]]
[[Category: Chen, Z.]]
[[Category: Davidson VL]]
[[Category: Davidson, V.L.]]
[[Category: Durley R]]
[[Category: Durley, R.]]
[[Category: Mathews FS]]
[[Category: Mathews, F.S.]]
[[Category: HEM]]
[[Category: NA]]
[[Category: amicyanin]]
[[Category: cytochrome]]
[[Category: electron transfer]]
[[Category: methylamine dehydrogenase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:06:53 2007''

Latest revision as of 12:38, 30 August 2023

Substrate reduced, copper free complex of methylamine dehydrogenase, amicyanin and cytochrome c551i from Paracoccus denitrificans.Substrate reduced, copper free complex of methylamine dehydrogenase, amicyanin and cytochrome c551i from Paracoccus denitrificans.

Structural highlights

2gc7 is a 16 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 1.9Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DHMH_PARDE Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin.

Evolutionary Conservation

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

See Also

2gc7, resolution 1.90Å

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