1hux
From Proteopedia
(New page: 200px<br /><applet load="1hux" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hux, resolution 3.0Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1hux.gif|left|200px]]<br /><applet load="1hux" size=" | + | [[Image:1hux.gif|left|200px]]<br /><applet load="1hux" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hux, resolution 3.0Å" /> | caption="1hux, resolution 3.0Å" /> | ||
'''CRYSTAL STRUCTURE OF THE ACIDAMINOCOCCUS FERMENTANS (R)-2-HYDROXYGLUTARYL-COA DEHYDRATASE COMPONENT A'''<br /> | '''CRYSTAL STRUCTURE OF THE ACIDAMINOCOCCUS FERMENTANS (R)-2-HYDROXYGLUTARYL-COA DEHYDRATASE COMPONENT A'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Acidaminococcus fermentans degrades glutamate via the hydroxyglutarate | + | Acidaminococcus fermentans degrades glutamate via the hydroxyglutarate pathway, which involves the syn-elimination of water from (R)-2-hydroxyglutaryl-CoA in a key reaction of the pathway. This anaerobic process is catalyzed by 2-hydroxyglutaryl-CoA dehydratase, an enzyme with two components (A and D) that reversibly associate during reaction cycles. Component A (CompA), a homodimeric protein of 2x27 kDa, contains a single, bridging [4Fe-4S] cluster and uses the hydrolysis of ATP to deliver an electron to the dehydratase component (CompD), where the electron is used catalytically. The structure of the extremely oxygen-sensitive CompA protein was solved by X-ray crystallography to 3 A resolution. The protein was found to be a member of the actin fold family, revealing a similar architecture and nucleotide-binding site. The key differences between CompA and other members of the actin fold family are: (i) the presence of a cluster binding segment, the "cluster helix"; (ii) the [4Fe-4S] cluster; and (iii) the location of the homodimer interface, which involves the bridging cluster. Possible reaction mechanisms are discussed in light of the close structural similarity to members of the actin-fold family and the functional similarity to the nitrogenase Fe- protein. |
==About this Structure== | ==About this Structure== | ||
| - | 1HUX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Acidaminococcus_fermentans Acidaminococcus fermentans] with SF4 and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1HUX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Acidaminococcus_fermentans Acidaminococcus fermentans] with <scene name='pdbligand=SF4:'>SF4</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HUX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Buckel, W.]] | [[Category: Buckel, W.]] | ||
[[Category: Hans, M.]] | [[Category: Hans, M.]] | ||
| - | [[Category: Locher, K | + | [[Category: Locher, K P.]] |
| - | [[Category: Rees, D | + | [[Category: Rees, D C.]] |
[[Category: Schmid, B.]] | [[Category: Schmid, B.]] | ||
| - | [[Category: Yeh, A | + | [[Category: Yeh, A P.]] |
[[Category: ADP]] | [[Category: ADP]] | ||
[[Category: SF4]] | [[Category: SF4]] | ||
[[Category: actin fold]] | [[Category: actin fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:05:04 2008'' |
Revision as of 11:05, 21 February 2008
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CRYSTAL STRUCTURE OF THE ACIDAMINOCOCCUS FERMENTANS (R)-2-HYDROXYGLUTARYL-COA DEHYDRATASE COMPONENT A
Overview
Acidaminococcus fermentans degrades glutamate via the hydroxyglutarate pathway, which involves the syn-elimination of water from (R)-2-hydroxyglutaryl-CoA in a key reaction of the pathway. This anaerobic process is catalyzed by 2-hydroxyglutaryl-CoA dehydratase, an enzyme with two components (A and D) that reversibly associate during reaction cycles. Component A (CompA), a homodimeric protein of 2x27 kDa, contains a single, bridging [4Fe-4S] cluster and uses the hydrolysis of ATP to deliver an electron to the dehydratase component (CompD), where the electron is used catalytically. The structure of the extremely oxygen-sensitive CompA protein was solved by X-ray crystallography to 3 A resolution. The protein was found to be a member of the actin fold family, revealing a similar architecture and nucleotide-binding site. The key differences between CompA and other members of the actin fold family are: (i) the presence of a cluster binding segment, the "cluster helix"; (ii) the [4Fe-4S] cluster; and (iii) the location of the homodimer interface, which involves the bridging cluster. Possible reaction mechanisms are discussed in light of the close structural similarity to members of the actin-fold family and the functional similarity to the nitrogenase Fe- protein.
About this Structure
1HUX is a Single protein structure of sequence from Acidaminococcus fermentans with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the Acidaminococcus fermentans 2-hydroxyglutaryl-CoA dehydratase component A., Locher KP, Hans M, Yeh AP, Schmid B, Buckel W, Rees DC, J Mol Biol. 2001 Mar 16;307(1):297-308. PMID:11243821
Page seeded by OCA on Thu Feb 21 13:05:04 2008
Categories: Acidaminococcus fermentans | Single protein | Buckel, W. | Hans, M. | Locher, K P. | Rees, D C. | Schmid, B. | Yeh, A P. | ADP | SF4 | Actin fold
