1ru3: Difference between revisions

New page: left|200px<br /><applet load="1ru3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ru3, resolution 2.20Å" /> '''Crystal Structure of...
 
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[[Image:1ru3.jpg|left|200px]]<br /><applet load="1ru3" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1ru3.jpg|left|200px]]<br /><applet load="1ru3" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1ru3, resolution 2.20&Aring;" />
caption="1ru3, resolution 2.20&Aring;" />
'''Crystal Structure of the monomeric acetyl-CoA synthase from Carboxydothermus hydrogenoformans'''<br />
'''Crystal Structure of the monomeric acetyl-CoA synthase from Carboxydothermus hydrogenoformans'''<br />


==Overview==
==Overview==
In anaerobic microorganisms employing the acetyl-CoA pathway, acetyl-CoA, synthase (ACS) and CO dehydrogenase (CODH) form a complex (ACS/CODH) that, catalyzes the synthesis of acetyl-CoA from CO, a methyl group, and CoA., Previously, a [4Fe-4S] cubane bridged to a copper-nickel binuclear site, (active site cluster A of the ACS component) was identified in the, ACS(Mt)/CODH(Mt) from Moorella thermoacetica whereas another study, revealed a nickel-nickel site in the open form of ACS(Mt), and a, zink-nickel site in the closed form. The ACS(Ch) of the hydrogenogenic, bacterium Carboxydothermus hydrogenoformans was found to exist as an, 82.2-kDa monomer as well as in a 1:1 molar complex with the 73.3-kDa, CODHIII(Ch). Homogeneous ACS(Ch) and ACS(Ch)/CODHIII(Ch) catalyzed the, exchange between [1-(14)C]acetyl-CoA and (12)CO with specific activities, of 2.4 or 5.9 micromol of CO per min per mg, respectively, at 70 degrees C, and pH 6.0. They also catalyzed the synthesis of acetyl-CoA from CO, methylcobalamin, corrinoid iron-sulfur protein, and CoA with specific, activities of 0.14 or 0.91 micromol of acetyl-CoA formed per min per mg, respectively, at 70 degrees C and pH 7.3. The functional cluster A of, ACS(Ch) contains a Ni-Ni-[4Fe-4S] site, in which the positions proximal, and distal to the cubane are occupied by Ni ions. This result is apparent, from a positive correlation of the Ni contents and negative correlations, of the Cu or Zn contents with the acetyl-CoA/CO exchange activities of, different preparations of monomeric ACS(Ch), a 2.2-A crystal structure of, the dithionite-reduced monomer in an open conformation, and x-ray, absorption spectroscopy.
In anaerobic microorganisms employing the acetyl-CoA pathway, acetyl-CoA synthase (ACS) and CO dehydrogenase (CODH) form a complex (ACS/CODH) that catalyzes the synthesis of acetyl-CoA from CO, a methyl group, and CoA. Previously, a [4Fe-4S] cubane bridged to a copper-nickel binuclear site (active site cluster A of the ACS component) was identified in the ACS(Mt)/CODH(Mt) from Moorella thermoacetica whereas another study revealed a nickel-nickel site in the open form of ACS(Mt), and a zink-nickel site in the closed form. The ACS(Ch) of the hydrogenogenic bacterium Carboxydothermus hydrogenoformans was found to exist as an 82.2-kDa monomer as well as in a 1:1 molar complex with the 73.3-kDa CODHIII(Ch). Homogeneous ACS(Ch) and ACS(Ch)/CODHIII(Ch) catalyzed the exchange between [1-(14)C]acetyl-CoA and (12)CO with specific activities of 2.4 or 5.9 micromol of CO per min per mg, respectively, at 70 degrees C and pH 6.0. They also catalyzed the synthesis of acetyl-CoA from CO, methylcobalamin, corrinoid iron-sulfur protein, and CoA with specific activities of 0.14 or 0.91 micromol of acetyl-CoA formed per min per mg, respectively, at 70 degrees C and pH 7.3. The functional cluster A of ACS(Ch) contains a Ni-Ni-[4Fe-4S] site, in which the positions proximal and distal to the cubane are occupied by Ni ions. This result is apparent from a positive correlation of the Ni contents and negative correlations of the Cu or Zn contents with the acetyl-CoA/CO exchange activities of different preparations of monomeric ACS(Ch), a 2.2-A crystal structure of the dithionite-reduced monomer in an open conformation, and x-ray absorption spectroscopy.


==About this Structure==
==About this Structure==
1RU3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Carboxydothermus_hydrogenoformans Carboxydothermus hydrogenoformans] with NI, SF4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RU3 OCA].  
1RU3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Carboxydothermus_hydrogenoformans Carboxydothermus hydrogenoformans] with <scene name='pdbligand=NI:'>NI</scene>, <scene name='pdbligand=SF4:'>SF4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RU3 OCA].  


==Reference==
==Reference==
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[[Category: nickel]]
[[Category: nickel]]


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