6dr3 | pdb_00006dr3

Crystal structure of E. coli LpoA amino terminal domain

spinqualitylabelsall models 6dr3, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6dr3 is a 1 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.101Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LPOA_ECOLI Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1A (PBP1a). Stimulates transpeptidase activity of PBP1a in vitro. Publication Abstract from PubMed The bacterial periplasmic protein LpoA is an outer membrane lipoprotein and an activator for the cross-linking activity of PBP1A, a bifunctional peptidoglycan synthase. Previous structures of the amino-terminal (N) domain of LpoA showed it to consist entirely of helices and loops, with at least four tetratricopeptide-like repeats. Although the previously determined orthorhombic crystal structure of the N domain of Haemophilus influenzae LpoA showed a typical curved structure with a concave groove, an NMR structure of the same domain from Escherichia coli was relatively flat. Here, a crystal structure of the N domain of E. coli LpoA was determined to a resolution of 2.1 A and was found to be more similar to the H. influenzae crystal structure than to the E. coli NMR structure. To provide a quantitative description for these comparisons, the various structures were superimposed pairwise by fitting the first half of each structure to its pairwise partner and then calculating the rotation axis that would optimally superimpose the second half. Differences in both the magnitude of the rotation and the direction of the rotation axis were observed between different pairs of structures. A 1.35 A resolution structure of a monoclinic crystal form of the N domain of H. influenzae LpoA was also determined. In this structure, the subdomains rotate 10 degrees relative to those in the original orthorhombic H. influenzae crystal structure to further narrow the groove between the subdomains. To accommodate this, a bound chloride ion (in place of sulfate) allowed the closer approach of a helix that forms one side of the groove. Crystal structures of the amino-terminal domain of LpoA from Escherichia coli and Haemophilus influenzae.,Kelley A, Vijayalakshmi J, Saper MA Acta Crystallogr F Struct Biol Commun. 2019 May 1;75(Pt 5):368-376. doi:, 10.1107/S2053230X19004011. Epub 2019 Apr 26. PMID:31045566 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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