1tht

<table><tr><td colspan='2'>[[1tht]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tht OCA], [http://pdbe.org/1tht PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tht RCSB], [http://www.ebi.ac.uk/pdbsum/1tht PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tht ProSAT]</span></td></tr>

[[http://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.

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== 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>

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<div class="pdbe-citations 1tht" style="background-color:#fffaf0;"></div>

*[[Thioesterase|Thioesterase]]

[[Category: Achromobacter harveyi johnson and shunk 1936]]

[[Category: Derewenda, U]]

[[Category: Derewenda, Z S]]

[[Category: Ferri, S]]

[[Category: Lawson, D M]]

[[Category: Meighen, E A]]

[[Category: Serre, L]]

[[Category: Szitter, R]]

[[Category: Wei, Y]]

[[Category: Thioesterase]]