3tgo

Crystal structure of the E. coli BamCD complex

spinqualitylabelsall models 3tgo, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3tgo is a 4 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, GOL, K, NA, PO4 Related: 2yh6, 2laf, 2yhc, 3qky, 3sns Gene: b2595, JW2577, yfiO (ECOLI), b2477, dapX, JW2462, nlpB (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] [BAMC_ECOLI] Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex that stabilizes the interaction between the essential proteins BamA and BamD.[HAMAP-Rule:MF_00924] Publication Abstract from PubMed The beta-barrel assembly machinery (BAM) complex of Escherichia coli is a multiprotein machine that catalyzes the essential process of assembling outer membrane proteins. The BAM complex consists of five proteins: one membrane protein, BamA, and four lipoproteins, BamB, BamC, BamD, and BamE. Here, we report the first crystal structure of a Bam lipoprotein complex: the essential lipoprotein BamD in complex with the N-terminal half of BamC (BamC(UN) (Asp(28)-Ala(217)), a 73-residue-long unstructured region followed by the N-terminal domain). The BamCD complex is stabilized predominantly by various hydrogen bonds and salt bridges formed between BamD and the N-terminal unstructured region of BamC. Sequence and molecular surface analyses revealed that many of the conserved residues in both proteins are found at the BamC-BamD interface. A series of truncation mutagenesis and analytical gel filtration chromatography experiments confirmed that the unstructured region of BamC is essential for stabilizing the BamCD complex structure. The unstructured N terminus of BamC interacts with the proposed substrate-binding pocket of BamD, suggesting that this region of BamC may play a regulatory role in outer membrane protein biogenesis. Crystal Structure of beta-Barrel Assembly Machinery BamCD Protein Complex.,Kim KH, Aulakh S, Paetzel M J Biol Chem. 2011 Nov 11;286(45):39116-21. Epub 2011 Sep 20. PMID:21937441 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Bam complex 3D structures

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