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3q6b

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The high-resolution and new form crystal structure of BamA POTRA4-5 from E.coli

Structural highlights

3q6b is a 1 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.5Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BAMA_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 BamD, the core component of the assembly machinery.^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

In Escherichia coli, the BAM complex is employed to mediate correct folding of the outer membrane (OM) proteins into beta-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 A resolution with an R factor of 14.7% and an R(free) of 18.9%.

High-resolution structure of a new crystal form of BamA POTRA4-5 from Escherichia coli.,Zhang H, Gao ZQ, Hou HF, Xu JH, Li LF, Su XD, Dong YH Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jul 1;67(Pt, 7):734-8. Epub 2011 Jun 23. PMID:21795783^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Doerrler WT, Raetz CR. Loss of outer membrane proteins without inhibition of lipid export in an Escherichia coli YaeT mutant. J Biol Chem. 2005 Jul 29;280(30):27679-87. Epub 2005 Jun 10. PMID:15951436 doi:http://dx.doi.org/M504796200
↑ Werner J, Misra R. YaeT (Omp85) affects the assembly of lipid-dependent and lipid-independent outer membrane proteins of Escherichia coli. Mol Microbiol. 2005 Sep;57(5):1450-9. PMID:16102012 doi:http://dx.doi.org/MMI4775
↑ Malinverni JC, Werner J, Kim S, Sklar JG, Kahne D, Misra R, Silhavy TJ. YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli. Mol Microbiol. 2006 Jul;61(1):151-64. PMID:16824102 doi:http://dx.doi.org/10.1111/j.1365-2958.2006.05211.x
↑ Hagan CL, Kim S, Kahne D. Reconstitution of outer membrane protein assembly from purified components. Science. 2010 May 14;328(5980):890-2. doi: 10.1126/science.1188919. Epub 2010 Apr, 8. PMID:20378773 doi:10.1126/science.1188919
↑ Hagan CL, Kahne D. The reconstituted Escherichia coli Bam complex catalyzes multiple rounds of beta-barrel assembly. Biochemistry. 2011 Sep 6;50(35):7444-6. doi: 10.1021/bi2010784. Epub 2011 Aug 11. PMID:21823654 doi:10.1021/bi2010784
↑ Zhang H, Gao ZQ, Hou HF, Xu JH, Li LF, Su XD, Dong YH. High-resolution structure of a new crystal form of BamA POTRA4-5 from Escherichia coli. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jul 1;67(Pt, 7):734-8. Epub 2011 Jun 23. PMID:21795783 doi:10.1107/S1744309111014254