1tht: Difference between revisions

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-[[Image:1tht.jpg|left|200px]]<br /><applet load="1tht" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1tht, resolution 2.1&Aring;" />
-'''STRUCTURE OF A MYRISTOYL-ACP-SPECIFIC THIOESTERASE FROM VIBRIO HARVEYI'''<br />
-==Overview==
+==STRUCTURE OF A MYRISTOYL-ACP-SPECIFIC THIOESTERASE FROM VIBRIO HARVEYI==
-The crystal structure of a myristoyl acyl carrier protein specific thioesterase (C14ACP-TE) from a bioluminescent bacterium, Vibrio harveyi, was solved by multiple isomorphous replacement methods and refined to an R factor of 22% at 2.1-A resolution. This is the first elucidation of a three-dimensional structure of a thioesterase. The overall tertiary architecture of the enzyme resembles closely the consensus fold of the rapidly expanding superfamily of alpha/beta hydrolases, although there is no detectable homology with any of its members at the amino acid sequence level. Particularly striking similarity exists between the C14ACP-TE structure and that of haloalkane dehalogenase from Xanthobacter autotrophicus. Contrary to the conclusions of earlier studies [Ferri, S. R., &amp; Meighen, E. A. (1991) J. Biol. Chem. 266, 12852-12857] which implicated Ser77 in catalysis, the crystal structure of C14ACP-TE reveals a lipase-like catalytic triad made up of Ser114, His241, and Asp211. Surprisingly, the gamma-turn with Ser114 in a strained secondary conformation (phi = 53 degrees, psi = -127 degrees), characteristic of the so-called nucleophilic elbow, does not conform to the frequently invoked lipase/esterase consensus sequence (Gly-X-Ser-X-Gly), as the positions of both glycines are occupied by larger amino acids. Site-directed mutagenesis and radioactive labeling support the catalytic function of Ser114. Crystallographic analysis of the Ser77--&gt;Gly mutant at 2.5-A resolution revealed no structural changes; in both cases the loop containing the residue in position 77 is disordered.(ABSTRACT TRUNCATED AT 250 WORDS)
+<StructureSection load='1tht' size='340' side='right'caption='[[1tht]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1tht]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_harveyi Vibrio harveyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1THT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1THT 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]] 2.1&#8491;</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=1tht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tht OCA], [https://pdbe.org/1tht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tht RCSB], [https://www.ebi.ac.uk/pdbsum/1tht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tht ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/LUXD_VIBHA LUXD_VIBHA] Acyl transferase is part of the fatty acid reductase system required for aldehyde biosynthesis; it produces fatty acids for the luminescent reaction.
+== 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/th/1tht_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=1tht ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-THT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_harveyi Vibrio harveyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1THT OCA].
+*[[Thioesterase 3D structures|Thioesterase 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Structure of a myristoyl-ACP-specific thioesterase from Vibrio harveyi., Lawson DM, Derewenda U, Serre L, Ferri S, Szittner R, Wei Y, Meighen EA, Derewenda ZS, Biochemistry. 1994 Aug 16;33(32):9382-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8068614 8068614]
+[[Category: Large Structures]]
-[[Category: Single protein]]
 [[Category: Vibrio harveyi]]
-[[Category: Derewenda, U.]]
+[[Category: Derewenda U]]
-[[Category: Derewenda, Z S.]]
+[[Category: Derewenda ZS]]
-[[Category: Ferri, S.]]
+[[Category: Ferri S]]
-[[Category: Lawson, D M.]]
+[[Category: Lawson DM]]
-[[Category: Meighen, E A.]]
+[[Category: Meighen EA]]
-[[Category: Serre, L.]]
+[[Category: Serre L]]
-[[Category: Szitter, R.]]
+[[Category: Szitter R]]
-[[Category: Wei, Y.]]
+[[Category: Wei Y]]
-[[Category: thioesterase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:13:45 2008''