Recombinant Streptomyces coelicolor Cobalt transport protein CbiN (cbiN)
Description
Introduction to Recombinant Streptomyces coelicolor Cobalt Transport Protein CbiN (cbiN)
The Recombinant Streptomyces coelicolor Cobalt transport protein CbiN (cbiN) is a crucial component of the Energy-Coupling Factor (ECF) transport system, specifically involved in the uptake of cobalt ions in bacteria. This protein is part of a larger complex that facilitates the transport of essential micronutrients across cell membranes. The CbiN protein is characterized as a membrane protein with two transmembrane helices connected by an extracytoplasmic loop, playing a pivotal role in enhancing cobalt transport activity when combined with other components like CbiM .
Structure and Function of CbiN
CbiN is a transmembrane protein with a specific structure that includes two transmembrane helices linked by an extracytoplasmic loop. This loop is crucial for its function, as any deletions within it can abolish transport activity . The protein is expressed in Streptomyces coelicolor, a bacterium known for its complex metabolic processes and secondary metabolite production .
| Characteristics of CbiN | Description |
|---|---|
| Protein Type | Transmembrane Protein |
| Function | Cobalt Transport |
| Structure | Two transmembrane helices with an extracytoplasmic loop |
| Expression System | In vitro E. coli expression system |
| Tag | N-terminal 10xHis-tagged |
Role in Cobalt Transport
CbiN interacts dynamically with other components of the ECF transporter system, such as CbiM, to facilitate cobalt uptake. The interaction between CbiN and CbiM involves loop-loop contacts that are essential for metal insertion into the binding pocket of the transporter . This interaction enhances the activity of the cobalt transporter, making it a critical auxiliary component for efficient cobalt transport.
Research Findings
Research on CbiN has highlighted its importance in cobalt transport. Studies have shown that CbiN can induce significant cobalt transport activity even in the absence of other components like CbiQO . The specific interaction between CbiN and CbiM has been characterized using techniques such as cysteine-scanning mutagenesis and crosslinking, confirming the predicted protein-protein contacts .
| Study Findings | Description |
|---|---|
| Cobalt Transport Activity | Enhanced by CbiN-CbiM interaction |
| Loop-Loop Interaction | Essential for metal insertion into the binding pocket |
| CbiN Deletions | Abolish transport activity if the extracytoplasmic loop is deleted |
Product Specs
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Note: All proteins are shipped with standard blue ice packs unless dry ice is specifically requested in advance. Dry ice shipments incur additional charges.
The tag type is determined during production. If you require a specific tag, please inform us, and we will prioritize its development.
Target Background
KEGG: sco:SCO5960
STRING: 100226.SCO5960
