2l5h | pdb_00002l5h

Solution Structure of the H189Q mutant of the Enzyme I dimer Using Residual Dipolar Couplings and Small Angle X-Ray Scattering

spinqualitylabelsall models 2l5h, 2 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2l5h is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2hwg, 3eza, 2wqd, 2hro, 2kx9, 2xdf Gene: ptsI, b2416, JW2409 ("Bacillus coli" Migula 1895) Activity: Phosphoenolpyruvate--protein phosphotransferase, with EC number 2.7.3.9 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PT1_ECOLI] General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr). Publication Abstract from PubMed The first component of the bacterial phosphotransferase system, enzyme I (EI), is a multidomain 128 kDa dimer that undergoes large rigid-body conformational transitions during the course of its catalytic cycle. Here we investigate the solution structure of a non-phosphorylatable active-site mutant in which the active-site histidine is substituted by glutamine. We show that perturbations in the relative orientations and positions of the domains and subdomains can be rapidly and reliably determined by conjoined rigid-body/torsion angle/Cartesian simulated annealing calculations driven by orientational restraints from residual dipolar couplings and shape and translation information afforded by small- and wide-angle X-ray scattering. Although histidine and glutamine are isosteric, the conformational space available to a Gln side chain is larger than that for the imidazole ring of His. An additional hydrogen bond between the side chain of Gln189 located on the EIN(alpha/beta) subdomain and an aspartate (Asp129) on the EIN(alpha) subdomain results in a small ( approximately 9 degrees ) reorientation of the EIN(alpha) and EIN(alpha/beta) subdomains that is in turn propagated to a larger reorientation ( approximately 26 degrees ) of the EIN domain relative to the EIC dimerization domain, illustrating the positional sensitivity of the EIN domain and its constituent subdomains to small structural perturbations. Combined Use of Residual Dipolar Couplings and Solution X-ray Scattering To Rapidly Probe Rigid-Body Conformational Transitions in a Non-phosphorylatable Active-Site Mutant of the 128 kDa Enzyme I Dimer.,Takayama Y, Schwieters CD, Grishaev A, Ghirlando R, Clore GM J Am Chem Soc. 2010 Dec 16. PMID:21162528 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphotransferase 3D structures

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