Beta-hydroxyacyl-acyl carrier protein dehydratase
From Proteopedia
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== Function == | == Function == | ||
| - | '''Beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase''' (FabZ) catalyzes the dehydration of short and long chained β-hydroxyacyl-ACPs. '''FabA''' exhibits broad overlapping activity to FabZ and is most active in dehydrating midlength chained β-hydroxyacyl-ACPs. | + | '''Beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase''' (FabZ) catalyzes the dehydration of short and long chained β-hydroxyacyl-ACPs. '''FabA''' exhibits broad overlapping activity to FabZ and is most active in dehydrating midlength chained β-hydroxyacyl-ACPs. |
== Structural highlights == | == Structural highlights == | ||
| - | The structure of FabA and FabZ shows a tunnel between the interfaces of the dimer. This tunnel accommodates the substrate. | + | <scene name='59/593305/Cv/2'>The structure of FabA and FabZ shows a tunnel between the interfaces of the dimer</scene>. This tunnel accommodates the substrate. <ref>PMID:16643907</ref> |
</StructureSection> | </StructureSection> | ||
Revision as of 13:54, 15 November 2015
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3D structures of β-hydroxyacyl-acyl carrier protein dehydratase
Updated on 15-November-2015
References
- ↑ Swarnamukhi PL, Sharma SK, Bajaj P, Surolia N, Surolia A, Suguna K. Crystal structure of dimeric FabZ of Plasmodium falciparum reveals conformational switching to active hexamers by peptide flips. FEBS Lett. 2006 May 15;580(11):2653-60. Epub 2006 Apr 21. PMID:16643907 doi:10.1016/j.febslet.2006.04.014
