1t2n

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[[Image:1t2n.jpg|left|200px]]
[[Image:1t2n.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1t2n |SIZE=350|CAPTION= <scene name='initialview01'>1t2n</scene>, resolution 1.80&Aring;
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The line below this paragraph, containing "STRUCTURE_1t2n", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= LIPA, LIP, BSU02700 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
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-->
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|DOMAIN=
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{{STRUCTURE_1t2n| PDB=1t2n | SCENE= }}
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|RELATEDENTRY=[[1t4m|1T4M]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t2n OCA], [http://www.ebi.ac.uk/pdbsum/1t2n PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t2n RCSB]</span>
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}}
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'''Structure of a thermostable triple mutant of Bacillus subtilis lipase obtained through directed evolution'''
'''Structure of a thermostable triple mutant of Bacillus subtilis lipase obtained through directed evolution'''
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[[Category: Rajakumara, E.]]
[[Category: Rajakumara, E.]]
[[Category: Sankaranarayanan, R.]]
[[Category: Sankaranarayanan, R.]]
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[[Category: alpha/beta hydrolase]]
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[[Category: Alpha/beta hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:26:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:50:24 2008''
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Revision as of 06:26, 3 May 2008

Image:1t2n.jpg

Template:STRUCTURE 1t2n

Structure of a thermostable triple mutant of Bacillus subtilis lipase obtained through directed evolution


Overview

Variation in gene sequences generated by directed evolution approaches often does not assure a minimalist design for obtaining a desired property in proteins. While screening for enhanced thermostability, structural information was utilized in selecting mutations that are generated by error-prone PCR. By this approach we have increased the half-life of denaturation by 300-fold compared to the wild-type Bacillus subtilis lipase through three point mutations generated by only two cycles of error-prone PCR. At lower temperatures the activity parameters of the thermostable mutants are unaltered. High-resolution crystal structures of the mutants show subtle changes, which include stacking of tyrosine residues, peptide plane flipping and a better anchoring of the terminus, that challenge rational design and explain the structural basis for enhanced thermostability. The approach may offer an efficient and minimalist solution for the enhancement of a desired property of a protein.

About this Structure

1T2N is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Structural basis of selection and thermostability of laboratory evolved Bacillus subtilis lipase., Acharya P, Rajakumara E, Sankaranarayanan R, Rao NM, J Mol Biol. 2004 Aug 27;341(5):1271-81. PMID:15321721 Page seeded by OCA on Sat May 3 09:26:27 2008

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