3q5m | pdb_00003q5m

Crystal structure of Escherichia coli BamD

spinqualitylabelsall models 3q5m, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3q5m is a 1 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: IOD Gene: yfiO (ECOLI) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [BAMD_ECOLI] Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamA, the core component of the assembly machinery. Probably involved in transient protein interactions.[HAMAP-Rule:MF_00922] Publication Abstract from PubMed The outer membrane protein complex (BAM complex) plays an important role in outer membrane protein (OMP) assembly in Escherichia coli. The BAM complex includes the integral beta-barrel protein BamA as well as four lipoproteins: BamB, BamC, BamD and BamE. One of these lipoproteins, BamD, is essential for the survival of Escherichia coli. The structure of BamD at 2.6 A resolution shows that this lipoprotein is composed of ten alpha-helices that form five tetratricopeptide-repeat (TPR) motifs. The arrangement of the BamD motifs is similar to that in the periplasmic part of BamA. One of the ten alpha-helices, alpha10, which has been shown to be important for the assembly of the BAM complex, is located in the very C-terminal region of BamD. A deep groove between TPR domains 4 and 5 is also observed. This groove, as well as the surface around alpha10, may provide binding sites for other components of the BAM complex. The C-terminal region of BamD serves as a platform for interactions with other components of the BAM complex. The N-terminal region shares structural similarity to other proteins whose functions are related to assistance in or regulation of secretion. Therefore, this region is likely to play an important role in the insertion of other outer membrane proteins. Structure of Escherichia coli BamD and its functional implications in outer membrane protein assembly.,Dong C, Hou HF, Yang X, Shen YQ, Dong YH Acta Crystallogr D Biol Crystallogr. 2012 Feb;68(Pt 2):95-101. Epub 2012 Jan 6. PMID:22281737 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Bam complex 3D structures

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