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4b7v

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Revision as of 14:14, 24 May 2017

Structure of wild type Pseudomonas aeruginosa FabF (KASII)

Structural highlights

4b7v is a 2 chain structure with sequence from Pseae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	[acyl-carrier-protein_synthase_II Beta-ketoacyl-[acyl-carrier-protein] synthase II], with EC number 2.3.1.179
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[O54440_PSEAI] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP (By similarity).[PIRNR:PIRNR000447]

Publication Abstract from PubMed

Bacterial infections remain a serious health concern, in particular causing life-threatening infections of hospitalized and immunocompromised patients. The situation is exacerbated by the rise in antibacterial drug resistance, and new treatments are urgently sought. In this endeavour, accurate structures of molecular targets can support early-stage drug discovery. Here, crystal structures, in three distinct forms, of recombinant Pseudomonas aeruginosa beta-ketoacyl-(acyl-carrier-protein) synthase II (FabF) are presented. This enzyme, which is involved in fatty-acid biosynthesis, has been validated by genetic and chemical means as an antibiotic target in Gram-positive bacteria and represents a potential target in Gram-negative bacteria. The structures of apo FabF, of a C164Q mutant in which the binding site is altered to resemble the substrate-bound state and of a complex with 3-(benzoylamino)-2-hydroxybenzoic acid are reported. This compound mimics aspects of a known natural product inhibitor, platensimycin, and surprisingly was observed binding outside the active site, interacting with a symmetry-related molecule. An unusual feature is a completely buried potassium-binding site that was identified in all three structures. Comparisons suggest that this may represent a conserved structural feature of FabF relevant to fold stability. The new structures provide templates for structure-based ligand design and, together with the protocols and reagents, may underpin a target-based drug-discovery project for urgently needed antibacterials.

Structures of Pseudomonas aeruginosa beta-ketoacyl-(acyl-carrier-protein) synthase II (FabF) and a C164Q mutant provide templates for antibacterial drug discovery and identify a buried potassium ion and a ligand-binding site that is an artefact of the crystal form.,Baum B, Lecker LS, Zoltner M, Jaenicke E, Schnell R, Hunter WN, Brenk R Acta Crystallogr F Struct Biol Commun. 2015 Aug 1;71(Pt 8):1020-6. doi:, 10.1107/S2053230X15010614. Epub 2015 Jul 28. PMID:26249693^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Baum B, Lecker LS, Zoltner M, Jaenicke E, Schnell R, Hunter WN, Brenk R. Structures of Pseudomonas aeruginosa beta-ketoacyl-(acyl-carrier-protein) synthase II (FabF) and a C164Q mutant provide templates for antibacterial drug discovery and identify a buried potassium ion and a ligand-binding site that is an artefact of the crystal form. Acta Crystallogr F Struct Biol Commun. 2015 Aug 1;71(Pt 8):1020-6. doi:, 10.1107/S2053230X15010614. Epub 2015 Jul 28. PMID:26249693 doi:http://dx.doi.org/10.1107/S2053230X15010614

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4b7v"

@@ Line 1: / Line 1: @@
 ==Structure of wild type Pseudomonas aeruginosa FabF (KASII)==
 <StructureSection load='4b7v' size='340' side='right' caption='[[4b7v]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-ketoacyl-[acyl-carrier-protein]_synthase_II Beta-ketoacyl-[acyl-carrier-protein] synthase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.179 2.3.1.179] </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=4b7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b7v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b7v RCSB], [http://www.ebi.ac.uk/pdbsum/4b7v PDBsum]</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=4b7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b7v OCA], [http://pdbe.org/4b7v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4b7v RCSB], [http://www.ebi.ac.uk/pdbsum/4b7v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4b7v ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4b7v" style="background-color:#fffaf0;"></div>
 ==See Also==

4b7v

From Proteopedia

Revision as of 14:14, 24 May 2017

Structure of wild type Pseudomonas aeruginosa FabF (KASII)

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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