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Enrichment of Bacterial Lipoproteins and Preparation of N-terminal Lipopeptides for Structural Determination by Mass Spectrometry
Published on: May 21, 2018
The lipocalin protein family: structural and sequence overview
D R Flower1, A C North, C E Sansom
1The Edward Jenner Institute for Vaccine Research, Newbury, Berkshire, UK. darren.flower@jenner.ac.uk
Biochimica Et Biophysica Acta
|November 4, 2000
Summary
Lipocalins exhibit diverse sequences but conserved structures, classified as kernel or outlier types. They belong to the calycins superfamily, sharing a common beta-barrel structure and signature.
Area of Science:
- Biochemistry
- Structural Biology
- Protein Science
Background:
- Lipocalins display significant sequence diversity.
- Lipocalins possess highly conserved structural features.
- Classification into kernel and outlier lipocalins aids family analysis.
Purpose of the Study:
- To analyze the sequence and structural diversity of lipocalins.
- To understand the relationship between lipocalins and the broader calycins superfamily.
- To identify conserved structural signatures within the calycins superfamily.
Main Methods:
- Sequence analysis to classify lipocalins.
- Structural analysis to identify conserved motifs.
- Comparative analysis with related protein families within the calycins superfamily.
Main Results:
- Lipocalins are classified into kernel (three motifs) and outlier (one or two motifs) groups.
- Smaller, highly similar sequence groups exist within these classifications.
- Lipocalins are part of the calycins superfamily, characterized by a conserved beta-barrel structure and signature.
Conclusions:
- The classification system effectively organizes lipocalin diversity.
- The calycins superfamily shares a common structural fold and signature.
- Structural conservation underlies the functional diversity of lipocalins.
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