1v35

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:43, 25 October 2023) (edit) (undo)
 
(13 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1v35.gif|left|200px]]
 
-
<!--
+
==Crystal Structure of Eoyl-ACP Reductase with NADH==
-
The line below this paragraph, containing "STRUCTURE_1v35", creates the "Structure Box" on the page.
+
<StructureSection load='1v35' size='340' side='right'caption='[[1v35]], [[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'>[[1v35]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V35 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=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr>
-
{{STRUCTURE_1v35| PDB=1v35 | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1v35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v35 OCA], [https://pdbe.org/1v35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v35 RCSB], [https://www.ebi.ac.uk/pdbsum/1v35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v35 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/Q9BJJ9_PLAFA Q9BJJ9_PLAFA]
 +
== 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/v3/1v35_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1v35 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Bacteria synthesize fatty acids in a dissociated type pathway different from that in humans. Enoyl acyl carrier protein reductase, which catalyzes the final step of fatty acid elongation, has been validated as a potential anti-microbial drug target. Triclosan is known to inhibit this enzyme effectively. Precise characterization of the mode of triclosan binding is required to develop highly specific inhibitors. With this in view, interactions between triclosan, the cofactor NADH/NAD+ and the enzyme from five different species, one plant and four of microbial origin, have been examined in the available crystal structures. A comparison of these structures shows major structural differences at the substrate/inhibitor/cofactor-binding loop. The analysis reveals that the conformation of this flexible loop and the binding affinities of triclosan to each of these enzymes are strongly correlated.
-
'''Crystal Structure of Eoyl-ACP Reductase with NADH'''
+
Structural basis for the variation in triclosan affinity to enoyl reductases.,Pidugu LS, Kapoor M, Surolia N, Surolia A, Suguna K J Mol Biol. 2004 Oct 8;343(1):147-55. PMID:15381426<ref>PMID:15381426</ref>
-
 
+
-
 
+
-
==Overview==
+
-
Bacteria synthesize fatty acids in a dissociated type pathway different from that in humans. Enoyl acyl carrier protein reductase, which catalyzes the final step of fatty acid elongation, has been validated as a potential anti-microbial drug target. Triclosan is known to inhibit this enzyme effectively. Precise characterization of the mode of triclosan binding is required to develop highly specific inhibitors. With this in view, interactions between triclosan, the cofactor NADH/NAD+ and the enzyme from five different species, one plant and four of microbial origin, have been examined in the available crystal structures. A comparison of these structures shows major structural differences at the substrate/inhibitor/cofactor-binding loop. The analysis reveals that the conformation of this flexible loop and the binding affinities of triclosan to each of these enzymes are strongly correlated.
+
-
==About this Structure==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
1V35 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V35 OCA].
+
</div>
 +
<div class="pdbe-citations 1v35" style="background-color:#fffaf0;"></div>
-
==Reference==
+
==See Also==
-
Structural basis for the variation in triclosan affinity to enoyl reductases., Pidugu LS, Kapoor M, Surolia N, Surolia A, Suguna K, J Mol Biol. 2004 Oct 8;343(1):147-55. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15381426 15381426]
+
*[[Enoyl-Acyl-Carrier Protein Reductase 3D structures|Enoyl-Acyl-Carrier Protein Reductase 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Plasmodium falciparum]]
[[Category: Plasmodium falciparum]]
-
[[Category: Single protein]]
+
[[Category: Kapoor M]]
-
[[Category: Kapoor, M.]]
+
[[Category: Suguna K]]
-
[[Category: Suguna, K.]]
+
[[Category: Surolia A]]
-
[[Category: Surolia, A.]]
+
[[Category: SwarnaMukhi PL]]
-
[[Category: SwarnaMukhi, P L.]]
+
[[Category: Surolia N]]
-
[[Category: Surolia, N.]]
+
-
[[Category: Enoyl-acp reductase]]
+
-
[[Category: Fabi]]
+
-
[[Category: Nadh]]
+
-
[[Category: P falciparum]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:01:10 2008''
+

Current revision

Crystal Structure of Eoyl-ACP Reductase with NADH

PDB ID 1v35

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1v35"
Personal tools