1y6h
From Proteopedia
(New page: 200px<br /><applet load="1y6h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y6h, resolution 2.20Å" /> '''Crystal structure of...) |
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| - | [[Image:1y6h.gif|left|200px]]<br /><applet load="1y6h" size=" | + | [[Image:1y6h.gif|left|200px]]<br /><applet load="1y6h" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1y6h, resolution 2.20Å" /> | caption="1y6h, resolution 2.20Å" /> | ||
'''Crystal structure of LIPDF'''<br /> | '''Crystal structure of LIPDF'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Peptide deformylase (PDF), which is essential for normal growth of | + | Peptide deformylase (PDF), which is essential for normal growth of bacteria but not for higher organisms, is explored as an attractive target for developing novel antibiotics. Here, we present the crystal structure of Leptospira interrogans PDF (LiPDF) at 2.2A resolution. To our knowledge, this is the first crystal structure of PDF associating in a stable dimer. The key loop (named the CD-loop: amino acid residues 66-76) near the active-site pocket adopts "closed" or "open" conformations in the two monomers forming the dimer. In the closed subunit, the CD-loop and residue Arg109 block the entry of the substrate-binding pocket, while the active-site pocket of the open subunit is occupied by the C-terminal tail from the neighbouring molecule. Moreover, a formate group, as one product of deformylisation, is observed bound with the active-site zinc ion. LiPDF displays significant structural differences in the C-terminal region compared to both type-I and type-II PDFs, suggesting a new family of PDFs. |
==About this Structure== | ==About this Structure== | ||
| - | 1Y6H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Leptospira_interrogans Leptospira interrogans] with ZN, GLY and FMT as [http://en.wikipedia.org/wiki/ligands ligands]. This structure | + | 1Y6H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Leptospira_interrogans Leptospira interrogans] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=GLY:'>GLY</scene> and <scene name='pdbligand=FMT:'>FMT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1RN5. 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=1Y6H OCA]. |
==Reference== | ==Reference== | ||
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[[Category: pdf]] | [[Category: pdf]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:02:13 2008'' |
Revision as of 14:02, 21 February 2008
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Crystal structure of LIPDF
Overview
Peptide deformylase (PDF), which is essential for normal growth of bacteria but not for higher organisms, is explored as an attractive target for developing novel antibiotics. Here, we present the crystal structure of Leptospira interrogans PDF (LiPDF) at 2.2A resolution. To our knowledge, this is the first crystal structure of PDF associating in a stable dimer. The key loop (named the CD-loop: amino acid residues 66-76) near the active-site pocket adopts "closed" or "open" conformations in the two monomers forming the dimer. In the closed subunit, the CD-loop and residue Arg109 block the entry of the substrate-binding pocket, while the active-site pocket of the open subunit is occupied by the C-terminal tail from the neighbouring molecule. Moreover, a formate group, as one product of deformylisation, is observed bound with the active-site zinc ion. LiPDF displays significant structural differences in the C-terminal region compared to both type-I and type-II PDFs, suggesting a new family of PDFs.
About this Structure
1Y6H is a Single protein structure of sequence from Leptospira interrogans with , and as ligands. This structure supersedes the now removed PDB entry 1RN5. Active as Peptide deformylase, with EC number 3.5.1.88 Full crystallographic information is available from OCA.
Reference
Unique structural characteristics of peptide deformylase from pathogenic bacterium Leptospira interrogans., Zhou Z, Song X, Li Y, Gong W, J Mol Biol. 2004 May 21;339(1):207-15. PMID:15123432
Page seeded by OCA on Thu Feb 21 16:02:13 2008
Categories: Leptospira interrogans | Peptide deformylase | Single protein | Gong, W. | Li, Y. | Song, X. | Zhou, Z. | FMT | GLY | ZN | Open and close conformation | Pdf
