2cbg: Difference between revisions

Line 4:

==Overview==

Many secondary metabolic peptides from bacteria and fungi are produced by, non-ribosomal peptide synthetases (NRPS) where the final step of, biosynthesis is often catalysed by designated thioesterase domains. Here, we report the 1.8A crystal structure of the fengycin thioesterase (FenTE), from Bacillus subtilis F29-3, which catalyses the regio- and, stereoselective release and macrocyclization of the antibiotic fengycin, from the NRPS template. A structure of the PMSF-inactivated FenTE domain, suggests the location of the oxyanion hole and the binding site of the, C-terminal residue l-Ile11 of the lipopeptide. Using a combination of, docking, molecular dynamics simulations and in vitro activity assays, a, model of the FenTE-fengycin complex was derived in which peptide, cyclization requires strategic interactions with residues lining the, active site canyon.

Many secondary metabolic peptides from bacteria and fungi are produced by non-ribosomal peptide synthetases (NRPS) where the final step of biosynthesis is often catalysed by designated thioesterase domains. Here, we report the 1.8A crystal structure of the fengycin thioesterase (FenTE) from Bacillus subtilis F29-3, which catalyses the regio- and stereoselective release and macrocyclization of the antibiotic fengycin from the NRPS template. A structure of the PMSF-inactivated FenTE domain suggests the location of the oxyanion hole and the binding site of the C-terminal residue l-Ile11 of the lipopeptide. Using a combination of docking, molecular dynamics simulations and in vitro activity assays, a model of the FenTE-fengycin complex was derived in which peptide cyclization requires strategic interactions with residues lining the active site canyon.

==About this Structure==

Line 13:

[[Category: Bacillus subtilis]]

[[Category: Single protein]]

[[Category: Essen, L.O.]]

[[Category: Essen, L O.]]

[[Category: Marahiel, M.A.]]

[[Category: Marahiel, M A.]]

[[Category: Samel, S.]]

[[Category: PMS]]

Line 23:

[[Category: phosphopantetheine]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun~~ Feb ~~3 10~~:33:37 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:46:54 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==Overview==
-Many secondary metabolic peptides from bacteria and fungi are produced by, non-ribosomal peptide synthetases (NRPS) where the final step of, biosynthesis is often catalysed by designated thioesterase domains. Here, we report the 1.8A crystal structure of the fengycin thioesterase (FenTE), from Bacillus subtilis F29-3, which catalyses the regio- and, stereoselective release and macrocyclization of the antibiotic fengycin, from the NRPS template. A structure of the PMSF-inactivated FenTE domain, suggests the location of the oxyanion hole and the binding site of the, C-terminal residue l-Ile11 of the lipopeptide. Using a combination of, docking, molecular dynamics simulations and in vitro activity assays, a, model of the FenTE-fengycin complex was derived in which peptide, cyclization requires strategic interactions with residues lining the, active site canyon.
+Many secondary metabolic peptides from bacteria and fungi are produced by non-ribosomal peptide synthetases (NRPS) where the final step of biosynthesis is often catalysed by designated thioesterase domains. Here, we report the 1.8A crystal structure of the fengycin thioesterase (FenTE) from Bacillus subtilis F29-3, which catalyses the regio- and stereoselective release and macrocyclization of the antibiotic fengycin from the NRPS template. A structure of the PMSF-inactivated FenTE domain suggests the location of the oxyanion hole and the binding site of the C-terminal residue l-Ile11 of the lipopeptide. Using a combination of docking, molecular dynamics simulations and in vitro activity assays, a model of the FenTE-fengycin complex was derived in which peptide cyclization requires strategic interactions with residues lining the active site canyon.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Bacillus subtilis]]
 [[Category: Single protein]]
-[[Category: Essen, L.O.]]
+[[Category: Essen, L O.]]
-[[Category: Marahiel, M.A.]]
+[[Category: Marahiel, M A.]]
 [[Category: Samel, S.]]
 [[Category: PMS]]
@@ Line 23: / Line 23: @@
 [[Category: phosphopantetheine]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:33:37 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:46:54 2008''