5b6p

Structure of the dodecameric type-II dehydrogenate dehydratase from Acinetobacter baumannii at 2.00 A resolutionStructure of the dodecameric type-II dehydrogenate dehydratase from Acinetobacter baumannii at 2.00 A resolution

Structural highlights 5b6p is a 12 chain structure with sequence from Acinetobacter baumannii ATCC 17978. This structure supersedes the now removed PDB entry 5iba. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AROQ_ACIBT Catalyzes a trans-dehydration via an enolate intermediate. Publication Abstract from PubMed Dehydroquinase (3-dehydroquinate dehydratase, DHQD, EC 4.2.1.10) catalyzes the conversion of dehydroquinate to dehydroshikimate. DHQD from Acinetobacter baumannii (AbDHQD) was cloned, expressed and purified to homogeneity. The binding studies showed that two compounds quinic acid and citrazinic acid bound to AbDHQD at micromolar concentrations. AbDHQD was crystallized using 30% PEG-3350, 50mM tris-HCl and 1.0M MgSO4 at pH 8.0. Crystals of AbDHQD were stabilized with 25% glycerol for data collection at 100K. The X-ray intensity data were collected to 2.0A resolution. Crystals belonged to monoclinic space group P21 with cell dimensions, a=82.3, b=95.3, c=132.3A and beta=95.7 degrees . The structure was solved with molecular replacement method and refined to values of 0.200 and 0.232 for Rcryst and Rfree factors. The structures of 12 crystallographically independent molecules in the asymmetry unit were identical with r.m.s shifts for the C(alpha) atoms ranging from 0.3A to 0.8A. They formed a dodecamer with four trimers arranged in a tetrahedral manner. The classical lid adopted an open conformation although a sulfate ion was observed in the substrate binding site. As a result of which, the compounds quinic acid and citrazinic acid could not bind to AbDHQD. Binding studies and structure determination of the recombinantly produced type-II 3-dehydroquinate dehydratase from Acinetobacter baumannii.,Iqbal N, Kumar M, Sharma P, Yadav SP, Kaur P, Sharma S, Singh TP Int J Biol Macromol. 2017 Jan;94(Pt A):459-465. doi:, 10.1016/j.ijbiomac.2016.10.049. Epub 2016 Oct 18. PMID:27769928 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Dehydroquinase 3D structures

spinqualitylabelsall models 5b6p, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image