surA Antibody

1. SurA cycles between distinct conformational and functional states during the bacterial outer membrane assembly process. PMID: 26728192
2. These findings suggest an autoinhibitory mechanism for regulation of SurA chaperone activity through interdomain interactions involving a proline isomerase domain. PMID: 23943764
3. mutational studies on SurA to identify residues that are critical for function were conducted; formation of disulfide bond in mutants has no observable detrimental effect on protein activity, indicating SurA does not undergo large-scale conformational change while performing its function PMID: 23275244
4. The results indicate that FimD usher follows the SurA-BamB pathway for its assembly. PMID: 21784935
5. Unfolded protein molecules initially form a highly dynamic complex with the chaperone domain of SlyD, and they are then transferred to the prolyl isomerase domain. PMID: 21147124
6. The biological importance of SurA was further substantiated by the finding that SurA also affects pathogenicity, being required for full virulence of uropathogenic Escherichia coli. PMID: 20447864
7. Data found that the periplasmic disulfide isomerase DsbC cooperates with SurA and the thiol oxidase DsbA in the folding of the essential beta-barrel protein LptD. PMID: 20615876
8. SurA was shown to be involved in the assembly of pili PMID: 16267292
9. 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 PMID: 17825319
10. SurA is the primary chaperone responsible for the periplasmic transit of the bulk mass of OMPs to the YaeT complex. PMID: 17908933
11. data support role for SurA in assembly of LptD & suggest that LptD is a true SurA substrate; based on results, we propose a revised model in which only a subset of outer membrane (OM) proteins depends on SurA for proper folding & insertion in the OM PMID: 19343722

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KEGG: ecj:JW0052

STRING: 316385.ECDH10B_0054