1ltg: Difference between revisions
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[[Image:1ltg.gif|left|200px]] | [[Image:1ltg.gif|left|200px]] | ||
'''THE ARG7LYS MUTANT OF HEAT-LABILE ENTEROTOXIN EXHIBITS GREAT FLEXIBILITY OF ACTIVE SITE LOOP 47-56 OF THE A SUBUNIT''' | {{Structure | ||
|PDB= 1ltg |SIZE=350|CAPTION= <scene name='initialview01'>1ltg</scene>, resolution 2.4Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''THE ARG7LYS MUTANT OF HEAT-LABILE ENTEROTOXIN EXHIBITS GREAT FLEXIBILITY OF ACTIVE SITE LOOP 47-56 OF THE A SUBUNIT''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1LTG is a [ | 1LTG is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LTG OCA]. | ||
==Reference== | ==Reference== | ||
The Arg7Lys mutant of heat-labile enterotoxin exhibits great flexibility of active site loop 47-56 of the A subunit., van den Akker F, Merritt EA, Pizza M, Domenighini M, Rappuoli R, Hol WG, Biochemistry. 1995 Sep 5;34(35):10996-1004. PMID:[http:// | The Arg7Lys mutant of heat-labile enterotoxin exhibits great flexibility of active site loop 47-56 of the A subunit., van den Akker F, Merritt EA, Pizza M, Domenighini M, Rappuoli R, Hol WG, Biochemistry. 1995 Sep 5;34(35):10996-1004. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7669757 7669757] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: enterotoxin]] | [[Category: enterotoxin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:34:57 2008'' | ||
Revision as of 13:34, 20 March 2008
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THE ARG7LYS MUTANT OF HEAT-LABILE ENTEROTOXIN EXHIBITS GREAT FLEXIBILITY OF ACTIVE SITE LOOP 47-56 OF THE A SUBUNIT
OverviewOverview
The heat-labile enterotoxin from Escherichia coli (LT) is a member of the cholera toxin family. These and other members of the larger class of AB5 bacterial toxins act through catalyzing the ADP-ribosylation of various intracellular targets including Gs alpha. The A subunit is responsible for this covalent modification, while the B pentamer is involved in receptor recognition. We report here the crystal structure of an inactive single-site mutant of LT in which arginine 7 of the A subunit has been replaced by a lysine residue. The final model contains 103 residues for each of the five B subunits, 175 residues for the A1 subunit, and 41 residues for the A2 subunit. In this Arg7Lys structure the active site cleft within the A subunit is wider by approximately 1 A than is seen in the wild-type LT. Furthermore, a loop near the active site consisting of residues 47-56 is disordered in the Arg7Lys structure, even though the new lysine residue at position 7 assumes a position which virtually coincides with that of Arg7 in the wild-type structure. The displacement of residues 47-56 as seen in the mutant structure is proposed to be necessary for allowing NAD access to the active site of the wild-type LT. On the basis of the differences observed between the wild-type and Arg7Lys structures, we propose a model for a coordinated sequence of conformational changes required for full activation of LT upon reduction of disulfide bridge 187-199 and cleavage of the peptide loop between the two cysteines in the A subunit.(ABSTRACT TRUNCATED AT 250 WORDS)
About this StructureAbout this Structure
1LTG is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
The Arg7Lys mutant of heat-labile enterotoxin exhibits great flexibility of active site loop 47-56 of the A subunit., van den Akker F, Merritt EA, Pizza M, Domenighini M, Rappuoli R, Hol WG, Biochemistry. 1995 Sep 5;34(35):10996-1004. PMID:7669757
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