1p42

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:05, 14 February 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='1p42' size='340' side='right'caption='[[1p42]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1p42' size='340' side='right'caption='[[1p42]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[1p42]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P42 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P42 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[1p42]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P42 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P42 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+
</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&#8491;</td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LPXC OR ENVA OR AQ_1772 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 "Aquifex aeolicus" Huber and Stetter 2001])</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p42 OCA], [https://pdbe.org/1p42 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p42 RCSB], [https://www.ebi.ac.uk/pdbsum/1p42 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p42 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p42 OCA], [https://pdbe.org/1p42 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p42 RCSB], [https://www.ebi.ac.uk/pdbsum/1p42 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p42 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/LPXC_AQUAE LPXC_AQUAE]] Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell (By similarity).
+
[https://www.uniprot.org/uniprot/LPXC_AQUAE LPXC_AQUAE] Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 20: Line 20:
</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=1p42 ConSurf].
</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=1p42 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
-
<div style="background-color:#fffaf0;">
 
-
== Publication Abstract from PubMed ==
 
-
The outer leaflet of the outer membrane of the Gram-negative bacterium serves as a permeability barrier and is composed of lipopolysaccharide, also known as endotoxin. The membrane anchor of lipopolysaccharide is lipid A, the biosynthesis of which is essential for cell viability. The first committed step in lipid A biosynthesis is catalyzed by UDP-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine deacetylase (LpxC), a zinc-dependent deacetylase. Here we report the crystal structure of LpxC from Aquifex aeolicus, which reveals a new alpha+beta fold reflecting primordial gene duplication and fusion, as well as a new zinc-binding motif. The catalytic zinc ion resides at the base of an active-site cleft and adjacent to a hydrophobic tunnel occupied by a fatty acid. This tunnel accounts for the specificity of LpxC toward substrates and inhibitors bearing appropriately positioned 3-O-fatty acid substituents. Notably, simple inhibitors designed to target interactions in the hydrophobic tunnel bind with micromolar affinity, thereby representing a step toward the structure-based design of a potent, broad-spectrum antibacterial drug.
 
- 
-
Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis.,Whittington DA, Rusche KM, Shin H, Fierke CA, Christianson DW Proc Natl Acad Sci U S A. 2003 Jul 8;100(14):8146-50. Epub 2003 Jun 20. PMID:12819349<ref>PMID:12819349</ref>
 
- 
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
-
</div>
 
-
<div class="pdbe-citations 1p42" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[UDP-3-O-acyl-N-acetylglucosamine deacetylase|UDP-3-O-acyl-N-acetylglucosamine deacetylase]]
*[[UDP-3-O-acyl-N-acetylglucosamine deacetylase|UDP-3-O-acyl-N-acetylglucosamine deacetylase]]
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Aquifex aeolicus huber and stetter 2001]]
+
[[Category: Aquifex aeolicus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Christianson, D W]]
+
[[Category: Christianson DW]]
-
[[Category: Fierke, C A]]
+
[[Category: Fierke CA]]
-
[[Category: Rusche, K M]]
+
[[Category: Rusche KM]]
-
[[Category: Shin, H]]
+
[[Category: Shin H]]
-
[[Category: Whittington, D A]]
+
[[Category: Whittington DA]]
-
[[Category: Alpha+beta fold]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Hydrophobic tunnel]]
+

Current revision

Crystal structure of Aquifex aeolicus LpxC Deacetylase (Zinc-Inhibited Form)

PDB ID 1p42

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools