4wuo

Structure of the E270A Mutant Isopropylmalate dehydrogenase from Thermus thermophilus in complex with IPM, Mn and NADH

spinqualitylabelsall models 4wuo, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4wuo is a 2 chain structure with sequence from Thermus thermophilus HB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.05Å Ligands: EOH, GOL, IPM, K, MN, NAD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LEU3_THET8 Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.[HAMAP-Rule:MF_01033] Publication Abstract from PubMed The mutant E270A of Thermus thermophilus 3-isopropylmalate dehydrogenase exhibits largely reduced ( approximately 1%) catalytic activity and negligible activation by K(+) compared to the wild-type enzyme. A 3-4kcal/mol increase in the activation energy of the catalysed reaction upon this mutation could also be predicted by QM/MM calculations. In the X-ray structure of the E270A mutant a water molecule was observed to take the place of K(+). SAXS and FRET experiments revealed the essential role of E270 in stabilisation of the active domain-closed conformation of the enzyme. In addition, E270 seems to position K(+) into close proximity of the nicotinamide ring of NAD(+) and the electron-withdrawing effect of K(+) may help to polarise the aromatic ring in order to aid the hydride-transfer. Glutamate 270 plays an essential role in K(+)-activation and domain closure of Thermus thermophilus isopropylmalate dehydrogenase.,Graczer E, Pallo A, Olah J, Szimler T, Konarev PV, Svergun DI, Merli A, Zavodszky P, Weiss MS, Vas M FEBS Lett. 2015 Jan 16;589(2):240-5. doi: 10.1016/j.febslet.2014.12.005. Epub, 2014 Dec 10. PMID:25497013 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Isopropylmalate dehydrogenase

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