'''STRUCTURE OF A MYRISTOYL-ACP-SPECIFIC THIOESTERASE FROM VIBRIO HARVEYI'''
===STRUCTURE OF A MYRISTOYL-ACP-SPECIFIC THIOESTERASE FROM VIBRIO HARVEYI===
==Overview==
<!--
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., & 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-->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)
The line below this paragraph, {{ABSTRACT_PUBMED_8068614}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 8068614 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_8068614}}
==About this Structure==
==About this Structure==
Line 31:
Line 35:
[[Category: Wei, Y.]]
[[Category: Wei, Y.]]
[[Category: Thioesterase]]
[[Category: Thioesterase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:57:52 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:45:12 2008''
Revision as of 10:45, 29 July 2008
This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.
1THT is a Single protein structure of sequence from Vibrio harveyi. Full crystallographic information is available from OCA.
Reference
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