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PMID: 7928990 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Characterization of a highly structured domain in Tbp2 from Neisseria meningitidis involved in binding to human transferrin.

Journal of bacteriology ·Vol. 176 ·No. 20 ·1994-10-00 ·Pages 6207-13

Vonder Haar RA, Legrain M, Kolbe HV, Jacobs E

Abstract

The binding of iron-loaded human transferrin at the surface of Neisseria meningitidis is mediated by two polypeptides, Tbp1 and Tbp2. Predicted Tbp amino acid sequences from N. meningitidis strains are highly divergent. This variability is particularly pronounced throughout the Tbp2 polypeptide. In this study, a highly structured and extremely stable Tbp2 domain of about 270 to 290 amino acids which is involved in the binding to transferrin and whose position is well conserved has been characterized. The conservation of such a remarkable structure in a very divergent protein domain (there is only 43% amino acid identity within this region) suggests that is plays an essential biological role and raises a number of questions regarding tbp2 evolution.

MeSH Terms
Amino Acid Sequence Base Sequence Carrier Proteins/genetics,metabolism DNA Mutational Analysis Escherichia coli/genetics Humans Iron-Binding Proteins Molecular Sequence Data Neisseria meningitidis/genetics,metabolism Open Reading Frames/genetics Protein Conformation Protein Denaturation Recombinant Proteins/metabolism Sequence Deletion Sequence Homology, Amino Acid Structure-Activity Relationship Transferrin/metabolism Transferrin-Binding Proteins
Chemicals
Carrier Proteins Iron-Binding Proteins Recombinant Proteins Transferrin Transferrin-Binding Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Vonder Haar R A
Transgène SA, Strasbourg, France.
Legrain M
Kolbe H V
Jacobs E
References (17)
17 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1994-10-00
Pages
6207-13
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC196960
Subset
IM
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