2okl: Difference between revisions

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==Overview==

Peptide deformylase (PDF) is a metalloenzyme that removes the N-terminal, formyl groups from newly synthesized proteins. It is essential for, bacterial survival, and is therefore-considered as a potential target for, antimicrobial chemotherapy. However, some bacteria including medically, relevant pathogens possess two or more def-like genes. Here we have, examined two PDFs from Bacillus cereus. The two share only 32% sequence, identity and the crystal structures show overall similarity with PDF2, having a longer C-terminus. However, there are differences at the two, active sites, and these differences appear to contribute to the activity, difference seen between the two. BcPDF2 is found as a dimer in the crystal, form with two additional actinonin bound at that interface.

Peptide deformylase (PDF) is a metalloenzyme that removes the N-terminal formyl groups from newly synthesized proteins. It is essential for bacterial survival, and is therefore-considered as a potential target for antimicrobial chemotherapy. However, some bacteria including medically relevant pathogens possess two or more def-like genes. Here we have examined two PDFs from Bacillus cereus. The two share only 32% sequence identity and the crystal structures show overall similarity with PDF2 having a longer C-terminus. However, there are differences at the two active sites, and these differences appear to contribute to the activity difference seen between the two. BcPDF2 is found as a dimer in the crystal form with two additional actinonin bound at that interface.

==About this Structure==

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[[Category: Peptide deformylase]]

[[Category: Single protein]]

[[Category: Kim, E.E.]]

[[Category: Kim, E E.]]

[[Category: BB2]]

[[Category: CIT]]

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[[Category: hydrolase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed Jan 23 11~~:05:57 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:19:30 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-Peptide deformylase (PDF) is a metalloenzyme that removes the N-terminal, formyl groups from newly synthesized proteins. It is essential for, bacterial survival, and is therefore-considered as a potential target for, antimicrobial chemotherapy. However, some bacteria including medically, relevant pathogens possess two or more def-like genes. Here we have, examined two PDFs from Bacillus cereus. The two share only 32% sequence, identity and the crystal structures show overall similarity with PDF2, having a longer C-terminus. However, there are differences at the two, active sites, and these differences appear to contribute to the activity, difference seen between the two. BcPDF2 is found as a dimer in the crystal, form with two additional actinonin bound at that interface.
+Peptide deformylase (PDF) is a metalloenzyme that removes the N-terminal formyl groups from newly synthesized proteins. It is essential for bacterial survival, and is therefore-considered as a potential target for antimicrobial chemotherapy. However, some bacteria including medically relevant pathogens possess two or more def-like genes. Here we have examined two PDFs from Bacillus cereus. The two share only 32% sequence identity and the crystal structures show overall similarity with PDF2 having a longer C-terminus. However, there are differences at the two active sites, and these differences appear to contribute to the activity difference seen between the two. BcPDF2 is found as a dimer in the crystal form with two additional actinonin bound at that interface.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Peptide deformylase]]
 [[Category: Single protein]]
-[[Category: Kim, E.E.]]
+[[Category: Kim, E E.]]
 [[Category: BB2]]
 [[Category: CIT]]
@@ Line 20: / Line 20: @@
 [[Category: hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:05:57 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:19:30 2008''