2gc4: Difference between revisions

Revision as of 18:30, 21 February 2008

Structural comparison of the oxidized ternary electron transfer complex of methylamine dehydrogenase, amicyanin and cytochrome c551i from Paracoccus denitrificans with the substrate-reduced, copper free complex at 1.9 A resolution.

OverviewOverview

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.

About this StructureAbout this Structure

2GC4 is a Protein complex structure of sequences from Paracoccus denitrificans with , and as ligands. Active as Amine dehydrogenase, with EC number 1.4.99.3 Full crystallographic information is available from OCA.

ReferenceReference

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:8140419

Page seeded by OCA on Thu Feb 21 17:30:19 2008

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OCA

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-[[Image:2gc4.gif|left|200px]]<br /><applet load="2gc4" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2gc4.gif|left|200px]]<br /><applet load="2gc4" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2gc4, resolution 1.90&Aring;" />
 '''Structural comparison of the oxidized ternary electron transfer complex of methylamine dehydrogenase, amicyanin and cytochrome c551i from Paracoccus denitrificans with the substrate-reduced, copper free complex at 1.9 A resolution.'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-GC4 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, 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=2GC4 OCA].
+GC4 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 <scene name='pdbligand=CU:'>CU</scene>, <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=HEM:'>HEM</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=2GC4 OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Protein complex]]
 [[Category: Chen, Z.]]
-[[Category: Davidson, V.L.]]
+[[Category: Davidson, V L.]]
 [[Category: Durley, R.]]
-[[Category: Mathews, F.S.]]
+[[Category: Mathews, F S.]]
 [[Category: CU]]
 [[Category: HEM]]
@@ Line 26: / Line 26: @@
 [[Category: methylamine dehydrogenase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:06:37 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:30:19 2008''