1j6t
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(New page: 200px<br /><applet load="1j6t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j6t" /> '''COMPLEX OF ENZYME IIAMTL AND THE HISTIDINE-C...)
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Revision as of 15:51, 20 November 2007
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COMPLEX OF ENZYME IIAMTL AND THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE
Overview
The solution structure of the complex between the cytoplasmic A domain, (IIA(Mtl)) of the mannitol transporter II(Mannitol) and the, histidine-containing phosphocarrier protein (HPr) of the Escherichia coli, phosphotransferase system has been solved by NMR, including the use of, conjoined rigid body/torsion angle dynamics, and residual dipolar, couplings, coupled with cross-validation, to permit accurate orientation, of the two proteins. A convex surface on HPr, formed by helices 1 and 2, interacts with a complementary concave depression on the surface of, IIA(Mtl) formed by helix 3, portions of helices 2 and 4, and beta-strands, 2 and 3. The majority of intermolecular contacts are hydrophobic, with a, small number of electrostatic interactions at the periphery of the, interface. The active site histidines, His-15 of HPr and His-65 of, IIA(Mtl), are in close spatial proximity, and a pentacoordinate phosphoryl, transition state can be readily accommodated with no change in, protein-protein orientation and only minimal perturbations of the backbone, immediately adjacent to the histidines. Comparison with two previously, solved structures of complexes of HPr with partner proteins of the, phosphotransferase system, the N-terminal domain of enzyme I (EIN) and, enzyme IIA(Glucose) (IIA(Glc)), reveals a number of common features, despite the fact that EIN, IIA(Glc), and IIA(Mtl) bear no structural, resemblance to one another. Thus, entirely different underlying structural, elements can form binding surfaces for HPr that are similar in terms of, both shape and residue composition. These structural comparisons, illustrate the roles of surface and residue complementarity, redundancy, incremental build-up of specificity and conformational side chain, plasticity in the formation of transient specific protein-protein, complexes in signal transduction pathways.
About this Structure
1J6T is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Solution structure of the phosphoryl transfer complex between the cytoplasmic A domain of the mannitol transporter IIMannitol and HPr of the Escherichia coli phosphotransferase system., Cornilescu G, Lee BR, Cornilescu CC, Wang G, Peterkofsky A, Clore GM, J Biol Chem. 2002 Nov 1;277(44):42289-98. Epub 2002 Aug 28. PMID:12202490
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