1cwu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1cwu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cwu, resolution 2.5&Aring;" /> '''BRASSICA NAPUS ENOYL ...)
Current revision (06:46, 7 February 2024) (edit) (undo)
 
(18 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1cwu.jpg|left|200px]]<br /><applet load="1cwu" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1cwu, resolution 2.5&Aring;" />
 
-
'''BRASSICA NAPUS ENOYL ACP REDUCTASE A138G MUTANT COMPLEXED WITH NAD+ AND THIENODIAZABORINE'''<br />
 
-
==Overview==
+
==BRASSICA NAPUS ENOYL ACP REDUCTASE A138G MUTANT COMPLEXED WITH NAD+ AND THIENODIAZABORINE==
-
Enoyl acyl carrier protein reductase (ENR) is involved in fatty acid, biosynthesis. In Escherichia coli this enzyme is the target for the, experimental family of antibacterial agents, the diazaborines, and for, triclosan, a broad spectrum antimicrobial agent. Biochemical studies have, suggested that the mechanism of diazaborine inhibition is dependent on, NAD(+) and not NADH, and resistance of Brassica napus ENR to diazaborines, is thought to be due to the replacement of a glycine in the active site of, the E. coli enzyme by an alanine at position 138 in the plant homologue., We present here an x-ray analysis of crystals of B. napus ENR A138G grown, in the presence of either NAD(+) or NADH and the structures of the, corresponding ternary complexes with thienodiazaborine obtained either by, soaking the drug into the crystals or by co-crystallization of the mutant, with NAD(+) and diazaborine. Analysis of the ENR A138G complex with, diazaborine and NAD(+) shows that the site of diazaborine binding is, remarkably close to that reported for E. coli ENR. However, the structure, of the ternary ENR A138G-NAD(+)-diazaborine complex obtained using, co-crystallization reveals a previously unobserved conformational change, affecting 11 residues that flank the active site and move closer to the, nicotinamide moiety making extensive van der Waals contacts with, diazaborine. Considerations of the mode of substrate binding suggest that, this conformational change may reflect a structure of ENR that is, important in catalysis.
+
<StructureSection load='1cwu' size='340' side='right'caption='[[1cwu]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1cwu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brassica_napus Brassica napus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CWU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CWU FirstGlance]. <br>
 +
</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=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=TDB:6-METHYL-2(PROPANE-1-SULFONYL)-2H-THIENO[3,2-D][1,2,3]DIAZABORININ-1-OL'>TDB</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=1cwu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cwu OCA], [https://pdbe.org/1cwu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cwu RCSB], [https://www.ebi.ac.uk/pdbsum/1cwu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cwu ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/FABI_BRANA FABI_BRANA] Catalyzes the NAD-dependent reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Catalyzes the last reduction step in the de novo synthesis cycle of fatty acids. Involved in the elongation cycle of fatty acids which are used in lipid metabolism. Required for normal plant growth (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/cw/1cwu_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=1cwu ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1CWU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Brassica_napus Brassica napus] with NAD and TDB as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Enoyl-[acyl-carrier-protein]_reductase_(NADH) Enoyl-[acyl-carrier-protein] reductase (NADH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.9 1.3.1.9] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CWU OCA].
+
*[[Enoyl-Acyl-Carrier Protein Reductase 3D structures|Enoyl-Acyl-Carrier Protein Reductase 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
Inhibitor binding studies on enoyl reductase reveal conformational changes related to substrate recognition., Roujeinikova A, Sedelnikova S, de Boer GJ, Stuitje AR, Slabas AR, Rafferty JB, Rice DW, J Biol Chem. 1999 Oct 22;274(43):30811-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10521472 10521472]
+
[[Category: Brassica napus]]
[[Category: Brassica napus]]
-
[[Category: Enoyl-[acyl-carrier-protein] reductase (NADH)]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Rafferty JB]]
-
[[Category: Rafferty, J.B.]]
+
[[Category: Rice DW]]
-
[[Category: Rice, D.W.]]
+
[[Category: Roujeinikova A]]
-
[[Category: Roujeinikova, A.]]
+
-
[[Category: NAD]]
+
-
[[Category: TDB]]
+
-
[[Category: diazaborine]]
+
-
[[Category: oxidoreductase]]
+
-
[[Category: plant lipid biosynthesis]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:48:47 2007''
+

Current revision

BRASSICA NAPUS ENOYL ACP REDUCTASE A138G MUTANT COMPLEXED WITH NAD+ AND THIENODIAZABORINE

PDB ID 1cwu

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/1cwu"
Personal tools