2pv2: Difference between revisions

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[[Image:2pv2.jpg|left|200px]]
{{Seed}}
[[Image:2pv2.png|left|200px]]


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{{STRUCTURE_2pv2|  PDB=2pv2  |  SCENE=  }}  
{{STRUCTURE_2pv2|  PDB=2pv2  |  SCENE=  }}  


'''Crystallographic Structure of SurA first peptidyl-prolyl isomerase domain complexed with peptide NFTLKFWDIFRK'''
===Crystallographic Structure of SurA first peptidyl-prolyl isomerase domain complexed with peptide NFTLKFWDIFRK===




==Overview==
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The periplasmic molecular chaperone protein SurA facilitates correct folding and maturation of outer membrane proteins in Gram-negative bacteria. It preferentially binds peptides that have a high fraction of aromatic amino acids. Phage display selections, isothermal titration calorimetry and crystallographic structure determination have been used to elucidate the basis of the binding specificity. The peptide recognition is imparted by the first peptidyl-prolyl isomerase (PPIase) domain of SurA. Crystal structures of complexes between peptides of sequence WEYIPNV and NFTLKFWDIFRK with the first PPIase domain of the Escherichia coli SurA protein at 1.3 A resolution, and of a complex between the dodecapeptide and a SurA fragment lacking the second PPIase domain at 3.4 A resolution, have been solved. SurA binds as a monomer to the heptapeptide in an extended conformation. It binds as a dimer to the dodecapeptide in an alpha-helical conformation, predicated on a substantial structural rearrangement of the SurA protein. In both cases, side-chains of aromatic residues of the peptides contribute a large fraction of the binding interactions. SurA therefore asserts a recognition preference for aromatic amino acids in a variety of sequence configurations by adopting alternative tertiary and quaternary structures to bind peptides in different conformations.
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{{ABSTRACT_PUBMED_17825319}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues., Xu X, Wang S, Hu YX, McKay DB, J Mol Biol. 2007 Oct 19;373(2):367-81. Epub 2007 Aug 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17825319 17825319]
The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues., Xu X, Wang S, Hu YX, McKay DB, J Mol Biol. 2007 Oct 19;373(2):367-81. Epub 2007 Aug 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17825319 17825319]
Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins., Bitto E, McKay DB, Structure. 2002 Nov;10(11):1489-98. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12429090 12429090]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Peptidylprolyl isomerase]]
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[[Category: Peptidyl-prolyl cis-trans isomerase domain]]
[[Category: Peptidyl-prolyl cis-trans isomerase domain]]
[[Category: Survival protein some]]
[[Category: Survival protein some]]
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