5jf4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "5jf4" [edit=sysop:move=sysop])
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 5jf4 is ON HOLD until Paper Publication
+
==Crystal structure of type 2 PDF from Streptococcus agalactiae in complex with inhibitor AT019==
 +
<StructureSection load='5jf4' size='340' side='right' caption='[[5jf4]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[5jf4]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JF4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JF4 FirstGlance]. <br>
 +
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6JT:(3R)-3-{3-[(1-BENZOFURAN-3-YL)METHYL]-1,2,4-OXADIAZOL-5-YL}-4-CYCLOPENTYL-N-HYDROXYBUTANAMIDE'>6JT</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 +
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></td></tr>
 +
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5jf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jf4 OCA], [http://pdbe.org/5jf4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jf4 RCSB], [http://www.ebi.ac.uk/pdbsum/5jf4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jf4 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[[http://www.uniprot.org/uniprot/DEF_STRA3 DEF_STRA3]] Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Peptide deformylase (PDF) is considered an excellent target to develop antibiotics. We have performed an extensive characterization of a new PDF from the pathogen Streptococcus agalactiae, showing properties similar to other known PDFs. S. agalactiae PDF could be used as PDF prototype as it allowed to get complete sets of 3-dimensional, biophysical and kinetic data with virtually any inhibitor compound. Structure-activity relationship analysis with this single reference system allowed us to reveal distinct binding modes for different PDF inhibitors and the key role of a hydrogen bond in potentiating the interaction between ligand and target. We propose this protein as an irreplaceable tool, allowing easy and relevant fine comparisons between series, to design, challenge and validate novel series of inhibitors. As proof-of-concept, we report here the design and synthesis of effective specific bacterial PDF inhibitors of an oxadiazole series with potent antimicrobial activity against a multidrug resistant clinical isolate.
-
Authors: Fieulaine, S., Giglione, C., Meinnel, T.
+
A unique peptide deformylase platform to rationally design and challenge novel active compounds.,Fieulaine S, Alves de Sousa R, Maigre L, Hamiche K, Alimi M, Bolla JM, Taleb A, Denis A, Pages JM, Artaud I, Meinnel T, Giglione C Sci Rep. 2016 Oct 20;6:35429. doi: 10.1038/srep35429. PMID:27762275<ref>PMID:27762275</ref>
-
Description: Crystal structure of type 2 PDF from Streptococcus agalactiae in complex with inhibitor AT019
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Unreleased Structures]]
+
</div>
-
[[Category: Meinnel, T]]
+
<div class="pdbe-citations 5jf4" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Peptide deformylase]]
[[Category: Fieulaine, S]]
[[Category: Fieulaine, S]]
[[Category: Giglione, C]]
[[Category: Giglione, C]]
 +
[[Category: Meinnel, T]]
 +
[[Category: At019]]
 +
[[Category: Hydrolase]]
 +
[[Category: Inhibitor]]
 +
[[Category: N-terminal methionine excision]]
 +
[[Category: Nme]]
 +
[[Category: Pdf]]
 +
[[Category: Streptococcus agalactiae]]
 +
[[Category: Type 2]]

Revision as of 18:34, 10 December 2016

Crystal structure of type 2 PDF from Streptococcus agalactiae in complex with inhibitor AT019

5jf4, resolution 2.40Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools