1v2g

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{{STRUCTURE_1v2g| PDB=1v2g | SCENE= }}
{{STRUCTURE_1v2g| PDB=1v2g | SCENE= }}
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'''The L109P mutant of E. coli Thioesterase I/Protease I/Lysophospholipase L1 (TAP) in complexed with octanoic acid'''
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===The L109P mutant of E. coli Thioesterase I/Protease I/Lysophospholipase L1 (TAP) in complexed with octanoic acid===
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==Overview==
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Escherichia coli thioesterase I/protease I/lysophospholipase L(1) (TAP) is a multifunctional lysophospholipase and acyl-CoA thioesterase with a SGNH-hydrolase fold. The relationship between TAP's structure and its versatile substrate specificity, however, is unclear. Here, we present the crystal structure of TAP in complex with octanoic acid (TAP-OCA; OCA, a free fatty acid with eight carbon atoms, C(8)). A structural comparison of native TAP with TAP-OCA reveals a remarkable conformational change in loop(75)(-)(80), called "switch loop movement", upon OCA binding to the substrate-binding crevice of TAP. OCA binding to the substrate-binding crevice results in a continuous hydrophobic surface, which triggers switch loop movement. The switch loop movement is acyl chain length dependent, with an effect of stabilizing the Michaelis complex (MC) of TAP during catalysis, and is essential for TAP's substrate preference. The finding of a sulfate ion binding site in the TAP structures, together with previous enzyme kinetic analyses, leads us to postulate that a putative CoA binding site is essential for efficient catalysis of thioesters in TAP. We also present the crystal structure of L109P-OCA (TAP's L109P mutant in complex with OCA), in which Leu109 mutated to Pro109 abolishes switch loop movement. This result strengthens our hypothesis that the switch loop movement is induced by hydrophobic interactions.
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(as it appears on PubMed at http://www.pubmed.gov), where 15697222 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15697222}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Substrate specificities of Escherichia coli thioesterase I/protease I/lysophospholipase L1 are governed by its switch loop movement., Lo YC, Lin SC, Shaw JF, Liaw YC, Biochemistry. 2005 Feb 15;44(6):1971-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15697222 15697222]
Substrate specificities of Escherichia coli thioesterase I/protease I/lysophospholipase L1 are governed by its switch loop movement., Lo YC, Lin SC, Shaw JF, Liaw YC, Biochemistry. 2005 Feb 15;44(6):1971-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15697222 15697222]
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Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network., Lo YC, Lin SC, Shaw JF, Liaw YC, J Mol Biol. 2003 Jul 11;330(3):539-51. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12842470 12842470]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Lo, Y C.]]
[[Category: Lo, Y C.]]
[[Category: Sgnh-hydrolase fold]]
[[Category: Sgnh-hydrolase fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:59:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:17:47 2008''

Revision as of 20:17, 27 July 2008

Image:1v2g.png

Template:STRUCTURE 1v2g

The L109P mutant of E. coli Thioesterase I/Protease I/Lysophospholipase L1 (TAP) in complexed with octanoic acid

Template:ABSTRACT PUBMED 15697222

About this Structure

1V2G is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Substrate specificities of Escherichia coli thioesterase I/protease I/lysophospholipase L1 are governed by its switch loop movement., Lo YC, Lin SC, Shaw JF, Liaw YC, Biochemistry. 2005 Feb 15;44(6):1971-9. PMID:15697222

Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network., Lo YC, Lin SC, Shaw JF, Liaw YC, J Mol Biol. 2003 Jul 11;330(3):539-51. PMID:12842470

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