Beta-hydroxyacyl-acyl carrier protein dehydratase

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== Function ==
== Function ==
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'''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. '''FabG''' is part of the fatty acid biosythesis elongation cycle. FabG reduces the β-keto acyl group of the elongating fatty acid<ref>PMID:11669613</ref>.
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'''Beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase''' or '''3-oxoacyl-ACP reductase''' (FabZ) catalyzes the dehydration of short and long chained β-hydroxyacyl-ACPs.
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*'''FabA''' exhibits broad overlapping activity to FabZ and is most active in dehydrating midlength chained β-hydroxyacyl-ACPs.
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*'''FabG''' or '''3-ketoacyl-(acyl-carrier-protein) reductase''' or '''beta-ketoacyl carrier protein reductase''' is part of the fatty acid biosythesis elongation cycle. FabG reduces the β-keto acyl group of the elongating fatty acid<ref>PMID:11669613</ref>.
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See also: [[Fatty acid synthesis]]
== Structural highlights ==
== Structural highlights ==
<scene name='59/593305/Cv/3'>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>
<scene name='59/593305/Cv/3'>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>
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</StructureSection>
 
==3D structures of β-hydroxyacyl-acyl carrier protein dehydratase==
==3D structures of β-hydroxyacyl-acyl carrier protein dehydratase==
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[[Beta-hydroxyacyl-acyl carrier protein dehydratase 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*FabZ
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**[[1u1z]] – PaFabZ – ''Pseudomonas aeruginosa''<br />
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**[[2gll]] – HpFabZ – ''Helicobacter pylori''<br />
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**[[2glv]] – HpFabZ (mutant)<br />
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**[[3d6x]] – FabZ – ''Campylobacter jejuni''<br />
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**[[4h4g]] – FabZ – ''Burkholderia thailandensis''<br />
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**[[4i83]] – FabZ – ''Neisseria meningitidis''<br />
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**[[1z6b]], [[2okh]], [[2oki]], [[1zhg]] – PfFabZ – ''Plasmodium falciparum''<br />
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**[[5buy]] – FabZ – ''Francisella tularensis''<br />
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**[[5bux]], [[5buw]] – FabZ – ''Yersinia pestis''<br />
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**[[4zw0]] – FabZ – ''Liberibacter asiaticus''<br />
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*FabZ complex
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**[[2glm]], [[2glp]], [[3b7j]], [[3cf8]], [[3cf9]], [[3d04]], [[3doy]], [[3doz]], [[3dp0]], [[3dp1]], [[3dp2]], [[3dp3]], [[3ed0]] – HpFabZ + inhibitor<br />
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**[[3az8]], [[3az9]], [[3aza]], [[3azb]] – PfFabZ + inhibitor<br />
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**[[4zjb]] – HpFabZ + acyl carrier protein<br />
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*FabA
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**[[1mkb]] – EcFabA – ''Escherichia coli''<br />
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**[[3q62]] – FabA – ''Yersinia pseudotuberculosis''<br />
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**[[4fq9]] – PaFabA <br />
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*FabA complex
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**[[1mka]] – EcFabA + 3-decynoyl-N-acetyl cysteamine <br />
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**[[4b8u]], [[4b0b]], [[4b0c]], [[4b0j]], [[4cl6]] – PaFabA + inhibitor<br />
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**[[4b0i]] – PaFabA (mutant) + inhibitor<br />
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**[[4keh]] – EcFabA + ACPP<br />
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*FabG
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**[[5end]] – FabG (mutant) – ''Vibrio cholerae''<br />
 
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**[[5ovj]] – MsFabG – ''Mycobacterium smegmatis''<br />
 
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**[[5ovk]], [[5ovl]] – MsFabG + NADPH<br />
 
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Structure of FabZ (PDB code 1zhg).

Drag the structure with the mouse to rotate

References

  1. ↑ Price AC, Zhang YM, Rock CO, White SW. Structure of beta-ketoacyl-[acyl carrier protein] reductase from Escherichia coli: negative cooperativity and its structural basis. Biochemistry. 2001 Oct 30;40(43):12772-81. PMID:11669613
  2. ↑ 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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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