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| - | [[Image:1gt6.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1gt6| PDB=1gt6 | SCENE= }} | | {{STRUCTURE_1gt6| PDB=1gt6 | SCENE= }} |
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| - | '''S146A MUTANT OF THERMOMYCES (HUMICOLA) LANUGINOSA LIPASE COMPLEX WITH OLEIC ACID'''
| + | ===S146A MUTANT OF THERMOMYCES (HUMICOLA) LANUGINOSA LIPASE COMPLEX WITH OLEIC ACID=== |
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| - | ==Overview==
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| - | The binding of Thermomyces lanuginosa lipase and its mutants [TLL(S146A), TLL(W89L), TLL(W117F, W221H, W260H)] to the mixed micelles of cis-parinaric acid/sodium taurodeoxycholate at pH 5.0 led to the quenching of the intrinsic tryptophan fluorescence emission (300-380 nm) and to a simultaneous increase in the cis-parinaric acid fluorescence emission (380-500 nm). These findings were used to characterize the Thermomyces lanuginosa lipase/cis-parinaric acid interactions occurring in the presence of sodium taurodeoxycholate.The fluorescence resonance energy transfer and Stern-Volmer quenching constant values obtained were correlated with the accessibility of the tryptophan residues to the cis-parinaric acid and with the lid opening ability of Thermomyces lanuginosa lipase (and its mutants). TLL(S146A) was found to have the highest fluorescence resonance energy transfer. In addition, a TLL(S146A)/oleic acid complex was crystallised and its three-dimensional structure was solved. Surprisingly, two possible binding modes (sn-1 and antisn1) were found to exist between oleic acid and the catalytic cleft of the open conformation of TLL(S146A). Both binding modes involved an interaction with tryptophan 89 of the lipase lid, in agreement with fluorescence resonance energy transfer experiments.As a consequence, we concluded that TLL(S146A) mutant is not an appropriate substitute for the wild-type Thermomyces lanuginosa lipase for mimicking the interaction between the wild-type enzyme and lipids. | + | The line below this paragraph, {{ABSTRACT_PUBMED_11895431}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11895431 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11895431}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Lipid degradation]] | | [[Category: Lipid degradation]] |
| | [[Category: Zymogen]] | | [[Category: Zymogen]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:58:37 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:02:05 2008'' |
Revision as of 03:02, 1 July 2008
Template:STRUCTURE 1gt6
S146A MUTANT OF THERMOMYCES (HUMICOLA) LANUGINOSA LIPASE COMPLEX WITH OLEIC ACID
Template:ABSTRACT PUBMED 11895431
About this Structure
1GT6 is a Single protein structure of sequence from Thermomyces lanuginosus. Full crystallographic information is available from OCA.
Reference
Binding of Thermomyces (Humicola) lanuginosa lipase to the mixed micelles of cis-parinaric acid/NaTDC., Yapoudjian S, Ivanova MG, Brzozowski AM, Patkar SA, Vind J, Svendsen A, Verger R, Eur J Biochem. 2002 Mar;269(6):1613-21. PMID:11895431
Page seeded by OCA on Tue Jul 1 06:02:05 2008
