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| | {{STRUCTURE_1tht| PDB=1tht | SCENE= }} | | {{STRUCTURE_1tht| PDB=1tht | SCENE= }} |
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| - | '''STRUCTURE OF A MYRISTOYL-ACP-SPECIFIC THIOESTERASE FROM VIBRIO HARVEYI'''
| + | ===STRUCTURE OF A MYRISTOYL-ACP-SPECIFIC THIOESTERASE FROM VIBRIO HARVEYI=== |
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| - | ==Overview==
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| - | 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. |
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| | + | {{ABSTRACT_PUBMED_8068614}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[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
Template:STRUCTURE 1tht
STRUCTURE OF A MYRISTOYL-ACP-SPECIFIC THIOESTERASE FROM VIBRIO HARVEYI
Template:ABSTRACT PUBMED 8068614
About this Structure
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
Page seeded by OCA on Tue Jul 29 13:45:12 2008
