2okl

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{{STRUCTURE_2okl| PDB=2okl | SCENE= }}
{{STRUCTURE_2okl| PDB=2okl | SCENE= }}
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'''Crystal structure of Peptide Deformylase 2 with actinonin from Bacillus cereus'''
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===Crystal structure of Peptide Deformylase 2 with actinonin from Bacillus cereus===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 18047803 is the PubMed ID number.
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{{ABSTRACT_PUBMED_18047803}}
==About this Structure==
==About this Structure==
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[[Category: Kim, E E.]]
[[Category: Kim, E E.]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:06:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:29:57 2008''

Revision as of 01:30, 28 July 2008

Image:2okl.png

Template:STRUCTURE 2okl

Crystal structure of Peptide Deformylase 2 with actinonin from Bacillus cereus

Template:ABSTRACT PUBMED 18047803

About this Structure

2OKL is a Single protein structure of sequence from Bacillus cereus. 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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