4e3e

CRYSTAL STRUCTURE OF putative MaoC domain protein dehydratase from Chloroflexus aurantiacus J-10-flCRYSTAL STRUCTURE OF putative MaoC domain protein dehydratase from Chloroflexus aurantiacus J-10-fl

Structural highlights

4e3e is a 2 chain structure with sequence from Chloroflexus aurantiacus J-10-fl. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MCH_CHLAA Involved in the glyoxylate assimilation cycle used to regenerate acetyl-CoA and produce pyruvate as universal precursor for biosynthesis. Catalyzes the reversible dehydration of beta-methylmalyl-CoA ((2R,3S)-beta-methylmalyl-CoA) to yield mesaconyl-CoA (methylfumaryl-CoA).^[1]

References

↑ Zarzycki J, Schlichting A, Strychalsky N, Muller M, Alber BE, Fuchs G. Mesaconyl-coenzyme A hydratase, a new enzyme of two central carbon metabolic pathways in bacteria. J Bacteriol. 2008 Feb;190(4):1366-74. Epub 2007 Dec 7. PMID:18065535 doi:http://dx.doi.org/10.1128/JB.01621-07

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OCA

[1] Zarzycki J, Schlichting A, Strychalsky N, Muller M, Alber BE, Fuchs G. Mesaconyl-coenzyme A hydratase, a new enzyme of two central carbon metabolic pathways in bacteria. J Bacteriol. 2008 Feb;190(4):1366-74. Epub 2007 Dec 7. PMID:18065535 doi:http://dx.doi.org/10.1128/JB.01621-07

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