4XGA
Crystal structure of BamB and BamA P3-5 complex from E.coli
Summary for 4XGA
| Entry DOI | 10.2210/pdb4xga/pdb |
| Descriptor | Outer membrane protein assembly factor BamB, Outer membrane protein assembly factor BamA, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | outer member protein, protein binding-membrane protein complex, protein binding/membrane protein |
| Biological source | Escherichia coli (strain K12) More |
| Cellular location | Cell outer membrane ; Lipid-anchor : P77774 Cell outer membrane : P0A940 |
| Total number of polymer chains | 2 |
| Total formula weight | 68065.00 |
| Authors | Chen, Z.,Zhan, L.H.,Dong, C.,Gao, Z.Q.,Dong, Y.H. (deposition date: 2014-12-30, release date: 2016-01-20, Last modification date: 2023-11-08) |
| Primary citation | Chen, Z.,Zhan, L.H.,Hou, H.F.,Gao, Z.Q.,Xu, J.H.,Dong, C.,Dong, Y.H. Structural basis for the interaction of BamB with the POTRA3-4 domains of BamA. Acta Crystallogr D Struct Biol, 72:236-244, 2016 Cited by PubMed Abstract: In Escherichia coli, the Omp85 protein BamA and four lipoproteins (BamBCDE) constitute the BAM complex, which is essential for the assembly and insertion of outer membrane proteins into the outer membrane. Here, the crystal structure of BamB in complex with the POTRA3-4 domains of BamA is reported at 2.1 Å resolution. Based on this structure, the POTRA3 domain is associated with BamB via hydrogen-bonding and hydrophobic interactions. Structural and biochemical analysis revealed that the conserved residues Arg77, Glu127, Glu150, Ser167, Leu192, Leu194 and Arg195 of BamB play an essential role in interaction with the POTRA3 domain. PubMed: 26894671DOI: 10.1107/S2059798315024729 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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