This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1hux
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1hux.gif|left|200px]] | [[Image:1hux.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1hux", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_1hux| PDB=1hux | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''CRYSTAL STRUCTURE OF THE ACIDAMINOCOCCUS FERMENTANS (R)-2-HYDROXYGLUTARYL-COA DEHYDRATASE COMPONENT A''' | '''CRYSTAL STRUCTURE OF THE ACIDAMINOCOCCUS FERMENTANS (R)-2-HYDROXYGLUTARYL-COA DEHYDRATASE COMPONENT A''' | ||
| Line 31: | Line 28: | ||
[[Category: Schmid, B.]] | [[Category: Schmid, B.]] | ||
[[Category: Yeh, A P.]] | [[Category: Yeh, A P.]] | ||
| - | [[Category: | + | [[Category: Actin fold]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:15:25 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 16:15, 2 May 2008
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. 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 Fri May 2 19:15:25 2008
