3qky | pdb_00003qky

Crystal structure of Rhodothermus marinus BamD

spinqualitylabelsall models 3qky, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3qky is a 1 chain structure with sequence from Rhodothermus marinus DSM 4252. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.15Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D0MFQ0_RHOM4 Publication Abstract from PubMed Folding and insertion of integral beta-barrel proteins in the outer membrane (OM) is an essential process for Gram-negative bacteria that requires the beta-barrel assembly machinery (BAM). Efficient OM protein (OMP) folding and insertion appears to require a consensus C-terminal signal in OMPs characterized by terminal F or W residues. The BAM complex is embedded in the OM and, in Escherichia coli, consists of the beta-barrel BamA and four lipoproteins BamBCDE. BamA and BamD are broadly distributed across all species of Gram-negative bacteria, whereas the other components are present in only a subset of species. BamA and BamD are also essential for viability, suggesting that these two proteins constitute the functional core of the bacterial BAM complex. Here, we present the crystal structure of BamD from the thermophilic bacteria Rhodothermus marinus refined to 2.15 A resolution. The protein contains five tetratricopeptide repeats (TPRs) organized into two offset tandems, each capped by a terminal helix. The N-terminal domain contains three TPRs and displays remarkable structural similarity with proteins that recognize targeting signals in extended conformations. The C-terminal domain harbors the remaining two TPRs and previously described mutations that impair binding to other BAM components map to this domain. Therefore, the structure suggests a model where the C-terminal domain provides a scaffold for interaction with BAM components, while the N-terminal domain participates in interaction with the substrates, either recognizing the C-terminal consensus sequence or binding unfolded OMP intermediates. Crystal Structure of BamD: An Essential Component of the beta-Barrel Assembly Machinery of Gram-Negative Bacteria.,Sandoval CM, Baker SL, Jansen K, Metzner SI, Sousa MC J Mol Biol. 2011 Apr 2. PMID:21463635 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Bam complex 3D structures

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