3pbi

Structure of the peptidoglycan hydrolase RipB (Rv1478) from Mycobacterium tuberculosis at 1.6 resolution

spinqualitylabelsall models 3pbi, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3pbi is a 1 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RIPB_MYCTU Peptidoglycan endopeptidase that cleaves the bond between D-glutamate and meso-diaminopimelate. Binds high-molecular weight peptidoglycan, but does not degrade it. Required for normal separation of daughter cells after cell division and cell wall integrity. Required for host cell invasion. Publication Abstract from PubMed The success of Mycobacterium tuberculosis in sustaining long-term survival within the host macrophages partly relies on its unique cell envelop that also confers low susceptibility to several antibiotics. Remodeling of the septal peptidoglycan (PG) has been linked to the putative PG hydrolases RipA and RipB. The crystal structures of RipB (Rv1478) and the homologous module of RipA (Rv1477) were determined to 1.60 A and 1.38 A resolution, respectively. Both proteins contain a C-terminal core domain resembling the NlpC-type PG hydrolases. However, the structure of RipB exhibits striking differences to the structures of this domain in RipA reported here and previously by others. Major structural differences were found in the N-terminal segments of 70 amino acids and in an adjacent loop, which form part of the substrate binding groove. Both RipA and RipB are able to bind PG. RipA, its C-terminal module and RipB cleave defined PG fragments between d-glutamate and meso-diaminopimelate with pH optima of 5 and 6, respectively. The peptidase module of RipA is also able to degrade Bacillus subtilis PG, which displays peptide stems and cross-links identical with those found in mycobacterial murein. RipB did not show comparable hydrolase activity with this substrate. Removal of the N-terminal segments previously suggested to have a role in auto-inhibition did not change the activity of either RipA or RipB. A comparison of the putative active-site clefts in the two enzymes provides structural insights into the basis of the differences in their substrate specificity. Peptidoglycan Remodeling in Mycobacterium tuberculosis: Comparison of Structures and Catalytic Activities of RipA and RipB.,Both D, Schneider G, Schnell R J Mol Biol. 2011 Oct 14;413(1):247-60. Epub 2011 Aug 16. PMID:21864539 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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