3Q6B
The high-resolution and new form crystal structure of BamA POTRA4-5 from E.coli
Summary for 3Q6B
| Entry DOI | 10.2210/pdb3q6b/pdb |
| Related | 3OG5 |
| Descriptor | Outer membrane protein assembly complex, YaeT protein (2 entities in total) |
| Functional Keywords | potra fold, insertion of outer membrane proteins, protein binding |
| Biological source | Escherichia coli |
| Cellular location | Cell outer membrane (By similarity): C9QRL1 |
| Total number of polymer chains | 1 |
| Total formula weight | 21353.91 |
| Authors | Gao, Z.Q.,Zhang, H.,Dong, Y.H. (deposition date: 2010-12-31, release date: 2011-08-10, Last modification date: 2023-11-01) |
| Primary citation | Zhang, H.,Gao, Z.Q.,Hou, H.F.,Xu, J.H.,Li, L.F.,Su, X.D.,Dong, Y.H. High-resolution structure of a new crystal form of BamA POTRA4-5 from Escherichia coli. Acta Crystallogr.,Sect.F, 67:734-738, 2011 Cited by PubMed Abstract: In Escherichia coli, the BAM complex is employed to mediate correct folding of the outer membrane (OM) proteins into β-barrels and their insertion into the OM. BamA, which is an essential component of the complex, consists of a C-terminal transmembrane region and five N-terminal polypeptide transport-associated (POTRA) domains. Although deletion studies have shown that each of the POTRA domains plays an important role in the process of BAM complex formation, only POTRA5 is essential for cell viability. Here, the crystal structure of POTRA4-5 has been determined to 1.50 Å resolution with an R factor of 14.7% and an Rfree of 18.9%. PubMed: 21795783DOI: 10.1107/S1744309111014254 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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