2ai8: Difference between revisions
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|PDB= 2ai8 |SIZE=350|CAPTION= <scene name='initialview01'>2ai8</scene>, resolution 1.700Å | |PDB= 2ai8 |SIZE=350|CAPTION= <scene name='initialview01'>2ai8</scene>, resolution 1.700Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene> | |LIGAND= <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SB7:[HYDROXY(3-PHENYLPROPYL)AMINO]METHANOL'>SB7</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Peptide_deformylase Peptide deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.88 3.5.1.88] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide_deformylase Peptide deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.88 3.5.1.88] </span> | ||
|GENE= def, fms ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= def, fms ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2ai7|2AI7]], [[2ai9|2AI9]], [[2aia|2AIA]], [[2aie|2AIE]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ai8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ai8 OCA], [http://www.ebi.ac.uk/pdbsum/2ai8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ai8 RCSB]</span> | |||
}} | }} | ||
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[[Category: Smith, K J.]] | [[Category: Smith, K J.]] | ||
[[Category: Smyth, M.]] | [[Category: Smyth, M.]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:53:03 2008'' | ||
Revision as of 01:53, 31 March 2008
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| , resolution 1.700Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | def, fms (Escherichia coli) | ||||||
| Activity: | Peptide deformylase, with EC number 3.5.1.88 | ||||||
| Related: | 2AI7, 2AI9, 2AIA, 2AIE
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
E.coli Polypeptide Deformylase complexed with SB-485343
OverviewOverview
Polypeptide deformylase (PDF) catalyzes the deformylation of polypeptide chains in bacteria. It is essential for bacterial cell viability and is a potential antibacterial drug target. Here, we report the crystal structures of polypeptide deformylase from four different species of bacteria: Streptococcus pneumoniae, Staphylococcus aureus, Haemophilus influenzae, and Escherichia coli. Comparison of these four structures reveals significant overall differences between the two Gram-negative species (E. coli and H. influenzae) and the two Gram-positive species (S. pneumoniae and S. aureus). Despite these differences and low overall sequence identity, the S1' pocket of PDF is well conserved among the four enzymes studied. We also describe the binding of nonpeptidic inhibitor molecules SB-485345, SB-543668, and SB-505684 to both S. pneumoniae and E. coli PDF. Comparison of these structures shows similar binding interactions with both Gram-negative and Gram-positive species. Understanding the similarities and subtle differences in active site structure between species will help to design broad-spectrum polypeptide deformylase inhibitor molecules.
About this StructureAbout this Structure
2AI8 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Structural variation and inhibitor binding in polypeptide deformylase from four different bacterial species., Smith KJ, Petit CM, Aubart K, Smyth M, McManus E, Jones J, Fosberry A, Lewis C, Lonetto M, Christensen SB, Protein Sci. 2003 Feb;12(2):349-60. PMID:12538898
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