1m5y

Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin FoldingCrystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin Folding

Structural highlights

1m5y is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SURA_ECOLI Chaperone involved in the correct folding and assembly of outer membrane proteins, such as OmpA, OmpF and LamB. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation. Essential for the survival of E.coli in stationary phase. Required for pilus biogenesis.^[1] ^[2] ^[3] ^[4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ Tormo A, Almiron M, Kolter R. surA, an Escherichia coli gene essential for survival in stationary phase. J Bacteriol. 1990 Aug;172(8):4339-47. PMID:2165476
↑ Rouviere PE, Gross CA. SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins. Genes Dev. 1996 Dec 15;10(24):3170-82. PMID:8985185
↑ Behrens S, Maier R, de Cock H, Schmid FX, Gross CA. The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity. EMBO J. 2001 Jan 15;20(1-2):285-94. PMID:11226178 doi:http://dx.doi.org/10.1093/emboj/20.1.285
↑ Justice SS, Hunstad DA, Harper JR, Duguay AR, Pinkner JS, Bann J, Frieden C, Silhavy TJ, Hultgren SJ. Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli. J Bacteriol. 2005 Nov;187(22):7680-6. PMID:16267292 doi:http://dx.doi.org/187/22/7680

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OCA

[1] Tormo A, Almiron M, Kolter R. surA, an Escherichia coli gene essential for survival in stationary phase. J Bacteriol. 1990 Aug;172(8):4339-47. PMID:2165476

[2] Rouviere PE, Gross CA. SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins. Genes Dev. 1996 Dec 15;10(24):3170-82. PMID:8985185

[3] Behrens S, Maier R, de Cock H, Schmid FX, Gross CA. The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity. EMBO J. 2001 Jan 15;20(1-2):285-94. PMID:11226178 doi:http://dx.doi.org/10.1093/emboj/20.1.285

[4] Justice SS, Hunstad DA, Harper JR, Duguay AR, Pinkner JS, Bann J, Frieden C, Silhavy TJ, Hultgren SJ. Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli. J Bacteriol. 2005 Nov;187(22):7680-6. PMID:16267292 doi:http://dx.doi.org/187/22/7680

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1m5y

Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin FoldingCrystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin Folding

Structural highlights

Function

Evolutionary Conservation

References

Contents

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1m5y

Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin FoldingCrystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin Folding

Structural highlights

Function

Evolutionary Conservation

References

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