Video Experimental Relacionado
Updated: Aug 8, 2026
10:43
Expression, Detergent Solubilization, and Purification of a Membrane Transporter, the MexB Multidrug Resistance Protein
Published on: December 3, 2010
Estructura del transportador de múltiples fármacos EmrD de Escherichia coli en el cuerpo humano
Yong Yin1, Xiao He, Paul Szewczyk
1Scripps Research Institute, Department of Molecular Biology, 10550 North Torrey Pines Road, CB-105, La Jolla, CA 92037, USA.
Science (New York, N.Y.)
|May 6, 2006
Resumen
La estructura de EmrD, un transportador multidroga de E. coli, revela un interior hidrofóbico y bucles que interactúan con la membrana. Estas características probablemente facilitan el transporte de moléculas anfipáticas desde la membrana celular.
Área de la Ciencia:
- Biología estructural Biología estructural.
- El transporte por membrana es el transporte por membrana.
- La bioquímica es la bioquímica.
Sus antecedentes:
- EmrD es un transportador de múltiples fármacos en Escherichia coli.
- Pertenece a la superfamilia de los Facilitadores Mayores.
- EmrD expulsa los compuestos anfipáticos a través de la membrana interna.
Objetivo del estudio:
- Para determinar la estructura de rayos X de EmrD.
- Para aclarar la base estructural de la función de transporte de EmrD.
Principales métodos:
- Cristalografía de rayos X con rayos X.
- Determinación de la estructura a una resolución de 3,5 angstroms.
Principales resultados:
- La estructura del EmrD revela una cavidad interna predominantemente hidrofóbica.
- Dos bucles extendidos se proyectan hacia el folleto interno de la membrana celular.
- Las regiones de la cavidad interna y del bucle están implicadas en la unión y el transporte del sustrato.
Conclusiones:
- La estructura determinada es consistente con el papel de EmrD en el transporte de moléculas anfipáticas.
- Las regiones del bucle pueden interactuar directamente con los sustratos de la bicapa lipídica y unirse a ellos.
- Es probable que EmrD utilice su cavidad interna y sus estructuras de bucle específicas para el reconocimiento y el transporte de múltiples substratos.
Más Videos Relacionados
Videos de Conceptos Relacionados
01:29Insertion of Multi-pass Transmembrane Proteins in the RER
The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
01:31ABC Transporters: Exporter
ATP-binding cassette or ABC transporter is the largest superfamily of integral membrane proteins. The transporters have transmembrane-binding domains (TMDs) and nucleotide-binding domains (NBDs). The TMDs are specific to their substrates, whereas the NBDs are similar to engines that complete ATP hydrolysis to complete the substrate transport. They can be full transporters consisting of two TMDs and NBDs, half transporters with one TMD and NBD, while some encoded with a single TMD or NBD are...
01:06Carrier-Mediated Transport
Carrier-mediated transport is a pivotal process in drug absorption, particularly for lipid-insoluble drugs, and encompasses facilitated diffusion and active transport. Facilitated diffusion allows drugs to move along their concentration gradient without energy expenditure, while active transport utilizes ATP to drive drug movement against this gradient.
Active transport involves two types of membrane-spanning transporters: uptake and efflux. Uptake transporters are expressed in the small...
Active transport involves two types of membrane-spanning transporters: uptake and efflux. Uptake transporters are expressed in the small...
01:28Protein Translocation Machinery on the ER Membrane
The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
01:27ABC Transporters: Importer
ATP-binding cassette or ABC transporters are a class of ATP-driven pumps that hydrolyze ATP to move solutes across the membrane. They can be grouped into importers and exporters. While exporters are present in all domains of life, importers exist only in bacteria and some plants.
In bacteria, based on the number of transmembrane helices and the chemical nature of their substrates, the ABC importers can be divided into three types:
In bacteria, based on the number of transmembrane helices and the chemical nature of their substrates, the ABC importers can be divided into three types:
01:26Insertion of Single-pass Transmembrane Proteins in the RER
Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...