NDLI: Cysteine scanning mutagenesis of the N-terminal 32 amino acid residues in the lactose permease of Escherichia coli.

Please wait, while we are loading the content...

Year: 2017 Volume: 26

Year: 2016 Volume: 25

Year: 2015 Volume: 24

Year: 2014 Volume: 23

Year: 2013 Volume: 22

Year: 2012 Volume: 21

Year: 2011 Volume: 20

Year: 2010 Volume: 19

Year: 2009 Volume: 18

Year: 2008 Volume: 17

Year: 2007 Volume: 16

Year: 2006 Volume: 15

Year: 2005 Volume: 14

Year: 2004 Volume: 13

Year: 2003 Volume: 12

Year: 2002 Volume: 11

Year: 2001 Volume: 10

Year: 2000 Volume: 9

Year: 1999 Volume: 8

Year: 1998 Volume: 7

Year: 1997 Volume: 6

Year: 1996 Volume: 5

Year: 1995 Volume: 4

Year: 1994 Volume: 3

Year: 1994 Volume: 3 Issue: 12

Year: 1994 Volume: 3 Issue: 11

Year: 1994 Volume: 3 Issue: 10

Year: 1994 Volume: 3 Issue: 9

Year: 1994 Volume: 3 Issue: 8

Year: 1994 Volume: 3 Issue: 7

Year: 1994 Volume: 3 Issue: 6

Year: 1994 Volume: 3 Issue: 5

Year: 1994 Volume: 3 Issue: 4

Year: 1994 Volume: 3 Issue: 3

Year: 1994 Volume: 3 Issue: 2

'Frozen' dynamic dimer model for transmembrane signaling in bacterial chemotaxis receptors.

Crystal structure of cholera toxin B-pentamer bound to receptor GM1 pentasaccharide.

cAMP-dependent protein kinase: crystallographic insights into substrate recognition and phosphotransfer.

Structure and dynamics of the active site gorge of acetylcholinesterase: synergistic use of molecular dynamics simulation and X-ray crystallography.

Sculpting proteins interactively: continual energy minimization embedded in a graphical modeling system.

Do salt bridges stabilize proteins? A continuum electrostatic analysis.

Role of the Cys 2-Cys 10 disulfide bond for the structure, stability, and folding kinetics of ribonuclease T1.

Cysteine scanning mutagenesis of the N-terminal 32 amino acid residues in the lactose permease of Escherichia coli.

Interaction of semisynthetic variants of RNase A with ribonuclease inhibitor.

Real-time DNA binding measurements of the ETS1 recombinant oncoproteins reveal significant kinetic differences between the p42 and p51 isoforms.

The native state of apomyoglobin described by proton NMR spectroscopy: interaction with the paramagnetic probe HyTEMPO and the fluorescent dye ANS.

Enzyme IIBcellobiose of the phosphoenol-pyruvate-dependent phosphotransferase system of Escherichia coli: backbone assignment and secondary structure determined by three-dimensional NMR spectroscopy.

An 1H NMR determination of the three-dimensional structures of mirror-image forms of a Leu-5 variant of the trypsin inhibitor from Ecballium elaterium (EETI-II).

The 2.6-A refined structure of the Escherichia coli recombinant Saccharomyces cerevisiae flavocytochrome b2-sulfite complex.

Characterization of a truncated form of arrestin isolated from bovine rod outer segments.

Sequence relationships between integral inner membrane proteins of binding protein-dependent transport systems: evolution by recurrent gene duplications.

Rational design of a three-heptad coiled-coil protein and comparison by molecular dynamics simulation with the GCN4 coiled coil: presence of interior three-center hydrogen bonds.

Conserved sequence pattern in a wide variety of phosphoesterases.

Acid sphingomyelinase possesses a domain homologous to its activator proteins: saposins B and D.

Year: 1994 Volume: 3 Issue: 1

Year: 1993 Volume: 2

Year: 1992 Volume: 1

Cysteine scanning mutagenesis of the N-terminal 32 amino acid residues in the lactose permease of Escherichia coli.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Schwieger, J. Kaback, H. R. Sahin-Tóth, M. Persson, B. Cohan, P.
Description	Author Affiliation: Sahin-Tóth M ( Howard Hughes Medical Institute, Department of Physiology, University of California at Los Angeles 90024-1662.)
Abstract	Using a functional lactose permease mutant devoid of Cys residues (C-less permease), each amino acid residue in the hydrophilic N-terminus and the first putative transmembrane helix was systematically replaced with Cys (from Tyr-2 to Trp-33). Twenty-three of 32 mutants exhibit high lactose accumulation (70-100% or more of C-less), and an additional 8 mutants accumulate to lower but highly significant levels. Surprisingly, Cys replacement for Gly-24 or Tyr-26 yields fully active permease molecules, and permease with Cys in place of Pro-28 also exhibits significant transport activity, although previous mutagenesis studies on these residues suggested that they may be required for lactose transport. As expected, Cys replacement for Pro-31 completely inactivates, in agreement with previous findings indicating that 'helix-breaking' propensity at this position is necessary for full activity (Consler TG, Tsolas O, Kaback HR, 1991, Biochemistry 30:1291-1297). Twenty-nine mutants are present in the membrane in amounts comparable to C-less permease, whereas membrane levels of mutants Tyr-3-->Cys and Phe-12-->Cys are slightly reduced, as judged by immunological techniques. Dramatically, mutant Phe-9-->Cys is hardly detectable when expressed from the lac promoter/operator at a relatively low rate, but is present in the membrane in a stable form when expressed at a high rate from the T7 promoter. Finally, studies with N-ethylmalemide show that 6 Cys-replacement mutants that cluster at the C-terminal end of putative helix I are inactivated significantly.(ABSTRACT TRUNCATED AT 250 WORDS)
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	2
Volume Number	3
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1994-02-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cysteine Escherichia Coli Proteins Escherichia Coli Enzymology Membrane Transport Proteins Chemistry Monosaccharide Transport Proteins Mutagenesis, Site-directed Symporters Amino Acid Sequence Biological Transport, Active Drug Effects Genetics Ethylmaleimide Pharmacology Kinetics Lactose Metabolism Molecular Sequence Data Protein Structure, Secondary Structure-activity Relationship Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

Central Library (ISO-9001:2015 Certified)
Indian Institute of Technology Kharagpur
Kharagpur, West Bengal, India | PIN - 721302

See location in the Map
03222 282435
Mail: support@ndl.gov.in

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in