2okl

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(New page: 200px<br /><applet load="2okl" size="350" color="white" frame="true" align="right" spinBox="true" caption="2okl, resolution 1.70&Aring;" /> '''Crystal structure of...)
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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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[[Category: Peptide deformylase]]
[[Category: Peptide deformylase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Kim, E.E.]]
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[[Category: Kim, E E.]]
[[Category: BB2]]
[[Category: BB2]]
[[Category: CIT]]
[[Category: CIT]]
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[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:05:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:19:30 2008''

Revision as of 16:19, 21 February 2008

Image:2okl.jpg

2okl, resolution 1.70Å

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Crystal structure of Peptide Deformylase 2 with actinonin from Bacillus cereus

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.

About this Structure

2OKL is a Single protein structure of sequence from Bacillus cereus with , and as ligands. Active as Peptide deformylase, with EC number 3.5.1.88 Full crystallographic information is available from OCA.

Reference

Characterization of peptide deformylase2 from B. cereus., Park JK, Kim KH, Moon JH, Kim EE, J Biochem Mol Biol. 2007 Nov 30;40(6):1050-7. PMID:18047803

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