3il6

From Proteopedia

(Difference between revisions)

Current revision

Structure of E. faecalis FabH in complex with 2-({4-[(3R,5S)-3,5-dimethylpiperidin-1-yl]-3-phenoxybenzoyl}amino)benzoic acid

Structural highlights

3il6 is a 1 chain structure with sequence from Enterococcus faecalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FABH_ENTFA Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

FabH (beta-ketoacyl-acyl carrier protein synthase III) is unique in that it initiates fatty acid biosynthesis, is inhibited by long-chain fatty acids providing means for feedback control of the process, and dictates the fatty acid profile of the organism by virtue of its substrate specificity. We report the crystal structures of bacterial FabH enzymes from four different pathogenic species: Enterococcus faecalis, Haemophilus influenzae, Staphylococcus aureus and Escherichia coli. Structural data on the enzyme from different species show important differences in the architecture of the substrate-binding sites that parallel the inter-species diversity in the substrate specificities of these enzymes.

Crystal structures of bacterial FabH suggest a molecular basis for the substrate specificity of the enzyme.,Gajiwala KS, Margosiak S, Lu J, Cortez J, Su Y, Nie Z, Appelt K FEBS Lett. 2009 Sep 3;583(17):2939-46. Epub 2009 Aug 6. PMID:19665020^[1]

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

References

↑ Gajiwala KS, Margosiak S, Lu J, Cortez J, Su Y, Nie Z, Appelt K. Crystal structures of bacterial FabH suggest a molecular basis for the substrate specificity of the enzyme. FEBS Lett. 2009 Sep 3;583(17):2939-46. Epub 2009 Aug 6. PMID:19665020 doi:10.1016/j.febslet.2009.08.001

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3il6"

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:3il6.png|left|200px]]
-<!--
+==Structure of E. faecalis FabH in complex with 2-({4-[(3R,5S)-3,5-dimethylpiperidin-1-yl]-3-phenoxybenzoyl}amino)benzoic acid==
-The line below this paragraph, containing "STRUCTURE_3il6", creates the "Structure Box" on the page.
+<StructureSection load='3il6' size='340' side='right'caption='[[3il6]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3il6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IL6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IL6 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B83:2-[({4-[(3R,5S)-3,5-DIMETHYLPIPERIDIN-1-YL]-3-PHENOXYPHENYL}CARBONYL)AMINO]BENZOIC+ACID'>B83</scene>, <scene name='pdbligand=SCY:S-ACETYL-CYSTEINE'>SCY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-{{STRUCTURE_3il6|  PDB=3il6  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3il6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3il6 OCA], [https://pdbe.org/3il6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3il6 RCSB], [https://www.ebi.ac.uk/pdbsum/3il6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3il6 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FABH_ENTFA FABH_ENTFA] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids (By similarity).
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/il/3il6_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3il6 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+FabH (beta-ketoacyl-acyl carrier protein synthase III) is unique in that it initiates fatty acid biosynthesis, is inhibited by long-chain fatty acids providing means for feedback control of the process, and dictates the fatty acid profile of the organism by virtue of its substrate specificity. We report the crystal structures of bacterial FabH enzymes from four different pathogenic species: Enterococcus faecalis, Haemophilus influenzae, Staphylococcus aureus and Escherichia coli. Structural data on the enzyme from different species show important differences in the architecture of the substrate-binding sites that parallel the inter-species diversity in the substrate specificities of these enzymes.
-===Structure of E. faecalis FabH in complex with 2-({4-[(3R,5S)-3,5-dimethylpiperidin-1-yl]-3-phenoxybenzoyl}amino)benzoic acid===
+Crystal structures of bacterial FabH suggest a molecular basis for the substrate specificity of the enzyme.,Gajiwala KS, Margosiak S, Lu J, Cortez J, Su Y, Nie Z, Appelt K FEBS Lett. 2009 Sep 3;583(17):2939-46. Epub 2009 Aug 6. PMID:19665020<ref>PMID:19665020</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3il6" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_19665020}}, adds the Publication Abstract to the page
+*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 19665020 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_19665020}}
+__TOC__
+</StructureSection>
-==About this Structure==
-IL6 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IL6 OCA].
-==Reference==
-<ref group="xtra">PMID:19665020</ref><references group="xtra"/>
-[[Category: Beta-ketoacyl-acyl-carrier-protein synthase III]]
 [[Category: Enterococcus faecalis]]
-[[Category: Appelt, K.]]
+[[Category: Large Structures]]
-[[Category: Cortez, J.]]
+[[Category: Appelt K]]
-[[Category: Gajiwala, K S.]]
+[[Category: Cortez J]]
-[[Category: Lu, J.]]
+[[Category: Gajiwala KS]]
-[[Category: Margosiak, S.]]
+[[Category: Lu J]]
-[[Category: Nie, Z.]]
+[[Category: Margosiak S]]
-[[Category: Su, Y.]]
+[[Category: Nie Z]]
-[[Category: Acyltransferase]]
+[[Category: Su Y]]
-[[Category: Antibiotic]]
-[[Category: Cytoplasm]]
-[[Category: Fabh]]
-[[Category: Fatty acid biosynthesis]]
-[[Category: Lipid synthesis]]
-[[Category: Multifunctional enzyme]]
-[[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Sep 21 19:31:13 2009''

3il6

From Proteopedia

Current revision

Structure of E. faecalis FabH in complex with 2-({4-[(3R,5S)-3,5-dimethylpiperidin-1-yl]-3-phenoxybenzoyl}amino)benzoic acid

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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