1tht: Difference between revisions

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 <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/"achromobacter_harveyi"_johnson_and_shunk_1936 "achromobacter harveyi" johnson and shunk 1936]. 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>
+<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='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>
+</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.
+[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]]
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 </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>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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)
-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:8068614<ref>PMID:8068614</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1tht" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Thioesterase 3D structures|Thioesterase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Achromobacter harveyi johnson and shunk 1936]]
 [[Category: Large Structures]]
-[[Category: Derewenda, U]]
+[[Category: Vibrio harveyi]]
-[[Category: Derewenda, Z S]]
+[[Category: Derewenda U]]
-[[Category: Ferri, S]]
+[[Category: Derewenda ZS]]
-[[Category: Lawson, D M]]
+[[Category: Ferri S]]
-[[Category: Meighen, E A]]
+[[Category: Lawson DM]]
-[[Category: Serre, L]]
+[[Category: Meighen EA]]
-[[Category: Szitter, R]]
+[[Category: Serre L]]
-[[Category: Wei, Y]]
+[[Category: Szitter R]]
-[[Category: Thioesterase]]
+[[Category: Wei Y]]