2ai9: Difference between revisions
New page: left|200px<br /><applet load="2ai9" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ai9, resolution 2.500Å" /> '''S.aureus Polypeptid... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2ai9.gif|left|200px]]<br /><applet load="2ai9" size=" | [[Image:2ai9.gif|left|200px]]<br /><applet load="2ai9" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2ai9, resolution 2.500Å" /> | caption="2ai9, resolution 2.500Å" /> | ||
'''S.aureus Polypeptide Deformylase'''<br /> | '''S.aureus Polypeptide Deformylase'''<br /> | ||
==Overview== | ==Overview== | ||
Polypeptide deformylase (PDF) catalyzes the deformylation of polypeptide | 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 Structure== | ==About this Structure== | ||
2AI9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with NI and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | 2AI9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=NI:'>NI</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AI9 OCA]. | ||
==Reference== | ==Reference== | ||
| Line 15: | Line 15: | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
[[Category: Aubart, K.]] | [[Category: Aubart, K.]] | ||
[[Category: Christensen, S | [[Category: Christensen, S B.]] | ||
[[Category: Fosberry, A.]] | [[Category: Fosberry, A.]] | ||
[[Category: Jones, J.]] | [[Category: Jones, J.]] | ||
| Line 21: | Line 21: | ||
[[Category: Lonetto, M.]] | [[Category: Lonetto, M.]] | ||
[[Category: McManus, E.]] | [[Category: McManus, E.]] | ||
[[Category: Petit, C | [[Category: Petit, C M.]] | ||
[[Category: Smith, K | [[Category: Smith, K J.]] | ||
[[Category: Smyth, M.]] | [[Category: Smyth, M.]] | ||
[[Category: NI]] | [[Category: NI]] | ||
| Line 28: | Line 28: | ||
[[Category: hudrolase]] | [[Category: hudrolase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:27:41 2008'' | ||
Revision as of 17:27, 21 February 2008
|
S.aureus Polypeptide Deformylase
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
2AI9 is a Single protein structure of sequence from Staphylococcus aureus with and as ligands. Active as Peptide deformylase, with EC number 3.5.1.88 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
Page seeded by OCA on Thu Feb 21 16:27:41 2008