5ah1

Structure of EstA from Clostridium botulinum

spinqualitylabelsall models 5ah1, resolution 1.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ah1 is a 1 chain structure with sequence from Clostridium botulinum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.2Å Ligands: K, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A5I055_CLOBH Publication Abstract from PubMed Two novel esterases from the anaerobe Clostridium botulinum ATCC 3502 (Cbotu_EstA and Cbotu_EstB) were expressed in Escherichia coli BL21-Gold(DE3) and were found to hydrolyze the polyester poly(butylene adipate-co-butylene terephthalate) (PBAT). The active site residues (triad Ser, Asp, His) are present in both enzymes at the same location only with some amino acid variations near the active site at the surrounding of aspartate. Yet, Cbotu_EstA showed higher kcat values on para-nitrophenyl butyrate and para-nitrophenyl acetate and was considerably more active (sixfold) on PBAT. The entrance to the active site of the modeled Cbotu_EstB appears more narrowed compared to the crystal structure of Cbotu_EstA and the N-terminus is shorter which could explain its lower activity on PBAT. The Cbotu_EstA crystal structure consists of two regions that may act as movable cap domains and a zinc metal binding site. Biotechnol. Bioeng. 2016;113: 1024-1034. (c) 2015 Wiley Periodicals, Inc. Hydrolysis of synthetic polyesters by Clostridium botulinum esterases.,Perz V, Baumschlager A, Bleymaier K, Zitzenbacher S, Hromic A, Steinkellner G, Pairitsch A, Lyskowski A, Gruber K, Sinkel C, Kuper U, Ribitsch D, Guebitz GM Biotechnol Bioeng. 2016 May;113(5):1024-34. doi: 10.1002/bit.25874. Epub 2015 Nov, 20. PMID:26524601 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Lipase 3D Structures

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