Kim, K Oh, J Han, D Kim, EE Lee, B Kim, Y 2024-01-21T03:37:16Z 2024-01-21T03:37:16Z 2021-09-01 2006-02-24 0006-291X https://pubs.kist.re.kr/handle/201004/135744 PilF is a requisite protein involved in the type 4 pilus biogenesis system from the Gram-negative human pathogenic bacteria, Pseudomonas aeruginosa. We determined the PilF structure at a 2.2 angstrom resolution; this includes six tandem tetratrico peptide repeat (TPR) units forming right-handed superhelix. PilF structure was similar to the heat shock protein organizing protein, which interacts with the C-terminal peptide of Hsp90 and Hsp70 via a concave Asn ladder in the inner groove of TPR superhelix. After simulated screening, the C-terminal pentapeptides of PilG, PilU, PilY, and PilZ proved to be a likely candidate binding to PilF, which are ones of 25 necessary components involved in the type 4 pilus biogenesis system. We proposed that PilF would be critical as a bridgehead in protein-protein interaction and thereby, PilF may bind a necessary molecule in type 4 pilus biogenesis system such as PilG, PilU, PilY, and PilZ. (c) 2005 Elsevier Inc. All rights reserved. English ACADEMIC PRESS INC ELSEVIER SCIENCE ELECTRON-DENSITY MAPS TWITCHING MOTILITY BACTERIAL PROLIPOPROTEIN FIMBRIAL BIOGENESIS REPEAT DOMAIN TPR DOMAINS TRANSFERASE PEPTIDE SYSTEM IDENTIFICATION Crystal structure of PilF: Functional implication in the type 4 pilus biogenesis in Pseudomonas aeruginosa Article 10.1016/j.bbrc.2005.12.108 1 BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.340, no.4, pp.1028 - 1038 BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 340 4 1028 1038 scie scopus 000235041500003 2-s2.0-30544453079 Biochemistry & Molecular Biology Biophysics Biochemistry & Molecular Biology Biophysics Article ELECTRON-DENSITY MAPS TWITCHING MOTILITY BACTERIAL PROLIPOPROTEIN FIMBRIAL BIOGENESIS REPEAT DOMAIN TPR DOMAINS TRANSFERASE PEPTIDE SYSTEM IDENTIFICATION TPR type 4 pilus Pseudomonas aeruginosa PilF crystal structure