Role of glycine residues in the structure and function of lactose permease, an Escherichia coli membrane transport protein

Biochemistry ◽  
1995 ◽  
Vol 34 (3) ◽  
pp. 1030-1039 ◽  
Author(s):  
Kirsten Jung ◽  
Heinrich Jung ◽  
Patrick Colacurcio ◽  
H. Ronald Kaback
Keyword(s):  
Escherichia Coli ◽  
Membrane Transport ◽  
Structure And Function ◽  
Transport Protein ◽  
Lactose Permease ◽  
Membrane Transport Protein ◽  
And Function

Role of proline residues in the structure and function of a membrane transport protein

Biochemistry ◽  
1991 ◽  
Vol 30 (5) ◽  
pp. 1291-1298 ◽  
Author(s):  
Thomas G. Consler ◽  
Orestes Tsolas ◽  
H. Ronald Kaback
Keyword(s):  
Membrane Transport ◽  
Structure And Function ◽  
Transport Protein ◽  
Membrane Transport Protein ◽  
And Function

Structure and function of Escherichia coli DnaB protein: Role of the N-terminal domain in helicase activity

Biochemistry ◽  
1994 ◽  
Vol 33 (37) ◽  
pp. 11307-11314 ◽  
Author(s):  
Subhasis B. Biswas ◽  
Pei-Hua Chen ◽  
Esther E. Biswas
Keyword(s):  
Escherichia Coli ◽  
Structure And Function ◽  
Helicase Activity ◽  
Terminal Domain ◽  
And Function

scholarly journals The cytoplasmic domain is essential for transport function of the integral membrane transport protein SLC4A11

2016 ◽  
Vol 310 (2) ◽  
pp. C161-C174 ◽  
Author(s):  
Sampath K. Loganathan ◽  
Chris M. Lukowski ◽  
Joseph R. Casey
Keyword(s):  
Membrane Transport ◽  
Fluorescent Protein ◽  
Strong Association ◽  
Transport Protein ◽  
Transport Function ◽  
Hek 293 ◽  
Hek 293 Cells ◽  
Membrane Transport Protein ◽  
293 Cells

Large cytoplasmic domains (CD) are a common feature among integral membrane proteins. In virtually all cases, these CD have a function (e.g., binding cytoskeleton or regulatory factors) separate from that of the membrane domain (MD). Strong associations between CD and MD are rare. Here we studied SLC4A11, a membrane transport protein of corneal endothelial cells, the mutations of which cause genetic corneal blindness. SLC4A11 has a 41-kDa CD and a 57-kDa integral MD. One disease-causing mutation in the CD, R125H, manifests a catalytic defect, suggesting a role of the CD in transport function. Expressed in HEK-293 cells without the CD, MD-SLC4A11 is retained in the endoplasmic reticulum, indicating a folding defect. Replacement of CD-SLC4A11 with green fluorescent protein did not rescue MD-SLC4A11, suggesting some specific role of CD-SLC4A11. Homology modeling revealed that the structure of CD-SLC4A11 is similar to that of the Cl−/HCO3−exchange protein AE1 (SLC4A1) CD. Fusion to CD-AE1 partially rescued MD-SLC4A11 to the cell surface, suggesting that the structure of CD-AE1 is similar to that of CD-SLC4A11. The CD-AE1-MD-SLC4a11 chimera, however, had no functional activity. We conclude that CD-SLC4A11 has an indispensable role in the transport function of SLC4A11. CD-SLC4A11 forms insoluble precipitates when expressed in bacteria, suggesting that the domain cannot fold properly when expressed alone. Consistent with a strong association between CD-SLC4A11 and MD-SLC4A11, these domains specifically associate when coexpressed in HEK-293 cells. We conclude that SLC4A11 is a rare integral membrane protein in which the CD has strong associations with the integral MD, which contributes to membrane transport function.

scholarly journals Role of Ca2+ in structure and function of Complex I from Escherichia coli

2011 ◽  
Vol 1807 (1) ◽  
pp. 36-41 ◽  
Author(s):  
Marina Verkhovskaya ◽  
Juho Knuuti ◽  
Mårten Wikström
Keyword(s):  
Escherichia Coli ◽  
Complex I ◽  
Structure And Function ◽  
And Function

Investigation of structure and function of lactose permease of Escherichia coli

1980 ◽  
Vol 8 (6) ◽  
pp. 675-676 ◽  
Author(s):  
KONRAD BEYREUTHER ◽  
BARBARA BIESELER ◽  
RUTH EHRING ◽  
GRIESSER HANS-WERNER ◽  
MARTIN MIESCHENDAHL ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Structure And Function ◽  
Lactose Permease ◽  
And Function
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